03/15/2021 Reppoting of GSC done I used Bonide(4-10-3) Root&Grow with iba! to lessen shock of transplant and heavy defoliating. Flipping to 12-12 today (the first clones will be for outdoors) made before and after videos of defoliation, and reppot. Blue Dream is cruising along nicely with a little LST bending of branches & stems,so all in all not a bad week..

Growing great. Smells good looks like its going to be be a nice physcodelic and strain. Smells sweet and spicy mostly like sttawberries.

My homework. Rubisco regeneration is intrinsically linked to nitrogen supply because Rubisco is a major sink for nitrogen in plants, typically accounting for 15% to over 25% of total leaf nitrogen. The regeneration phase itself consumes nitrogen through the synthesis of the Rubisco enzyme and associated proteins (like Rubisco activase), and overall nitrogen status heavily influences the efficiency of RuBP regeneration.Structural Component: Nitrogen is an essential building block for all proteins, and the sheer abundance of the Rubisco protein makes it the single largest storage of nitrogen in the leaf. Synthesis and Activity: Adequate nitrogen supply is crucial for the synthesis and maintenance of sufficient Rubisco enzyme and Rubisco activase (Rca), the regulatory protein responsible for maintaining Rubisco's active state. Nitrogen deficiency leads to a decrease in the content and activity of both Rubisco and Rca, which in turn limits the maximum carboxylation rate, Vmax, and the rate of RuBP regeneration Jmax, thus reducing overall photosynthetic capacity. Nitrogen Storage and Remobilization: Rubisco can act as a temporary nitrogen storage protein, which is degraded to remobilize nitrogen to other growing parts of the plant, especially under conditions of nitrogen deficiency or senescence. Nitrogen Use Efficiency (NUE): The allocation of nitrogen to Rubisco is a key determinant of a plant's photosynthetic nitrogen use efficiency (PNUE). In high-nitrogen conditions, plants may accumulate a surplus of Rubisco, which may not be fully activated, leading to a lower PNUE. Optimizing the amount and activity of Rubisco relative to nitrogen availability is a target for improving crop NUE. Photorespiration and Nitrogen Metabolism: Nitrogen metabolism is also linked to the photorespiration pathway (which competes with carboxylation at the Rubisco active site), particularly in the reassimilation of ammonia released during the process. To increase RuBisCO regeneration, which refers to the process of forming the CO2 acceptor molecule Ribulose-1,5-bisphosphate (RuBP) during photosynthesis, the primary methods involve optimizing the levels and activity of Rubisco activase (Rca) and enhancing the performance of other Calvin-Benson-Bassham (CBB) cycle enzymes. Biochemical and Environmental Approaches: Optimize Rubisco Activase (Rca) activity: Rca is a crucial chaperone protein that removes inhibitory sugar phosphates, such as CA1P (2-carboxy-D-arabinitol 1-phosphate), from the Rubisco active site, thus maintaining its catalytic competence. •Ensure optimal light conditions: Rca is light-activated via the chloroplast's redox status. Adequate light intensity ensures Rca can effectively maintain Rubisco in its active, carbamylated state. •Maintain optimal temperature: Rca is highly temperature-sensitive and can become unstable at moderately high temperatures (e.g., above 35°C/95F° in many C3 plants), which decreases its ability to activate Rubisco. Maintaining temperatures within the optimal range for a specific plant species is important. •Optimize Mg2+ concentration: Mg2+ is a key cofactor for both Rubisco carbamylation and Rca activity. In the light, Mg2+ concentration in the chloroplast stroma increases, promoting activation. •Manage ATP/ADP ratio: Rca activity depends on ATP hydrolysis and is inhibited by ADP. Conditions that maintain a high ATP/ADP ratio in the chloroplast stroma favor Rca activity. Enhance Calvin-Benson-Bassham (CBB) cycle enzyme activity: The overall rate of RuBP regeneration can be limited by other enzymes in the cycle. •Increase SBPase activity: Sedoheptulose-1,7-bisphosphatase (SBPase) is a key regulatory enzyme in the regeneration pathway, and increasing its activity can enhance RuBP regeneration and overall photosynthesis. •Optimize other enzymes: Overexpression of other CBB cycle enzymes such as fructose-1,6-bisphosphate aldolase (FBA) and triose phosphate isomerase (TPI) can also help to balance the metabolic flux and improve RuBP regeneration capacity. Magnesium ions, Mg2+, are specifically required for Rubisco activation because the cation plays a critical structural and chemical role in forming the active site: A specific lysine residue in the active site must be carbamylated by a CO2 molecule to activate the enzyme. The resulting negatively charged carbamyl group then facilitates the binding of the positively charged Mg2+ion. While other divalent metal ions like Mn2+ can bind to Rubisco, they alter the enzyme's substrate specificity and lead to dramatically lower activity or a higher rate of the non-productive oxygenation reaction compared to Mg2+, making them biologically unfavorable in the context of efficient carbon fixation. The concentration of Mg2+ in the chloroplast stroma naturally increases in the light due to ion potential balancing during ATP synthesis, providing a physiological mechanism to ensure the enzyme is activated when photosynthesis is possible. At the center of the porphyrin ring, nestled within its nitrogen atoms, is a Magnesium ion (Mg2+). This magnesium ion is crucial for the function of chlorophyll, and without it, the pigment cannot effectively capture and transfer light energy. Mg acts as a cofactor: Mg2+ binds to Rubisco after an activator CO2 molecule, forming a catalytically competent complex (Enzyme-CO2-Mg2+). High light + CO2) increases demand: Under high light (60 DLI is a very high intensity, potentially saturating) and high CO2, the plant's capacity for photosynthesis is high, and thus the demand for activated Rubisco and the necessary Mg2+ cofactor increases. Mg deficiency becomes limiting: If Mg2+ is deficient under these conditions, the higher levels of Rubisco and Rubisco activase produced cannot be fully activated, leading to lower photosynthetic rates and potential photo-oxidative damage. Optimal range: Studies show that adequate Mg2+ application can enhance Rubisco activation and stabilize net photosynthetic rates under stress conditions, but the required concentration is specific to the experimental setup. Monitoring is key: The most effective approach in a controlled environment is to monitor the plant's physiological responses e.g., leaf Mg2+ concentration, photosynthetic rate, Rubisco activation state, and adjust the nutrient solution/fertilizer to maintain adequate levels, rather than supplementing a fixed "extra" amount. In practice, this means ensuring that Mg2+ is not a limiting factor in the plant's standard nutrient solution when pushing the limits with high light and CO2. Applying Mg2+ through foliar spray is beneficial to Rubisco regeneration, particularly in alleviating the negative effects of magnesium (Mg) deficiency and high-temperature stress (HTS). While Mg can be leached from soil, within the plant it is considered a mobile nutrient, particularly in the phloem. Foliar-applied Mg is quickly absorbed by the leaves and can be translocate to other plant parts, including new growth and sink organs. Foliar application of: NATURES VERY OWN MgSO4 @ 15.0g L-1 in a spray bottle. Foliar sprays are often recommended as a rapid rescue measure for existing deficiencies or as a supplement during critical growth stages, when demand for Mg is high. Application in the early morning or late evening can improve absorption and prevent leaf burn. The starting point [of creativity] is curiosity: pondering why the default exists in the first place. We’re driven to question defaults when we experience vuja de, the opposite of déjà vu. Déjà vu occurs when we encounter something new, but it feels as if we’ve seen it before. Vuja de is the reverse—we face something familiar, but we see it with a fresh perspective that enables us to gain new insights into old problems.

Al started flowering. Stunted plant was removed. Good health for the now 4 plants. Weather is good but very windy. All plants need support. This plant grows very well but the stem and canopy are not balanced.

Longer warmer days

Beautiful plant

Ladies from the 2x3 moved over to the 2x2.

ANTHOCYANIN production is primarily controlled by the Cryptochrome (CR1) Photoreceptor ( !! UV and Blue Spectrums are primary drivers in the production of the pigment that replaces chlorophyll, isn't that awesome! 1. Diverse photoreceptors in plants Many civilizations, including the sun god of ancient Egypt, thought that the blessings of sunlight were the source of life. In fact, the survival of all life, including humans, is supported by the photosynthesis of plants that capture solar energy. Plants that perform photosynthesis have no means of transportation except for some algae. Therefore, it is necessary to monitor various changes in the external environment and respond appropriately to the place to survive. Among various environmental information, light is especially important information for plants that perform photosynthesis. In the process of evolution, plants acquired phytochrome, which mainly receives light in the red light region, and multiple blue light receptors, including his hytropin and phototropin, in order to sense the light environment. .. In addition to these, an ultraviolet light receptor named UVR8 was recently discovered. The latest image of the molecular structure and function of these various plant photoreceptors (Fig. 1), focusing on phytochrome and phototropin. Figure 1 Ultraviolet-visible absorption spectra of phytochrome, cryptochrome, phototropin, and UVR8. The dashed line represents each bioactive absorption spectrum. 2. Phytochrome; red-far red photoreversible molecular switch What is phytochrome? Phytochrome is a photochromic photoreceptor, and has two absorption types, a red light absorption type Pr (absorption maximum wavelength of about 665 nm) and a far-red light absorption type Pfr (730 nm). Reversible light conversion between the two by red light and far-red light, respectively(Fig. 1A, solid line and broken line). In general, Pfr is the active form that causes a physiological response. With some exceptions, phytochrome can be said to function as a photoreversible molecular switch. The background of the discovery is as follows. There are some types of plants that require light for germination (light seed germination). From that study, it was found that germination was induced by red light, the effect was inhibited by subsequent far-red light irradiation, and this could be repeated, and the existence of photoreceptors that reversibly photoconvert was predicted. In 1959, its existence was confirmed by the absorption spectrum measurement of the yellow sprout tissue, and it was named phytochrome. Why does the plant have a sensor to distinguish between such red light and far-red light? There is no big difference between the red and far-red light regions in the open-field spectrum of sunlight, but the proportion of red light is greatly reduced due to the absorption of chloroplasts in the shade of plants. Similar changes in light quality occur in the evening sunlight. Plants perceive this difference in light quality as the ratio of Pr and Pfr, recognize the light environment, and respond to it. Subsequent studies have revealed that it is responsible for various photomorphogenic reactions such as photoperiodic flowering induction, shade repellent, and deyellowing (greening). Furthermore, with the introduction of the model plant Arabidopsis thaliana (At) and the development of molecular biological analysis methods, research has progressed dramatically, and his five types of phytochromes (phyA-E) are present in Arabidopsis thaliana. all right. With the progress of the genome project, Fi’s tochrome-like photoreceptors were found in cyanobacteria, a photosynthetic prokaryotes other than plants. Furthermore, in non-photosynthetic bacteria, a homologue molecule called bacteriophytochrome photoreceptor (BphP) was found in Pseudomonas aeruginosa (Pa) and radiation-resistant bacteria (Deinococcus radiodurans, Dr). Domain structure of phytochrome molecule Phytochrome molecule can be roughly divided into N-terminal side and C-terminal side region. PAS (Per / Arndt / Sim: blue), GAF (cGMP phosphodiesterase / adenylyl cyclase / FhlA: green), PHY (phyto-chrome: purple) 3 in the N-terminal region of plant phytochrome (Fig. 2A) There are two domains and an N-terminal extension region (NTE: dark blue), and phytochromobilin (PΦB), which is one of the ring-opening tetrapyrroles, is thioether-bonded to the system stored in GAF as a chromophore. ing. PAS is a domain involved in the interaction between signal transduction-related proteins, and PHY is a phytochrome-specific domain. There are two PASs and her histidine kinase-related (HKR) domain (red) in the C-terminal region, but the histidine essential for kinase activity is not conserved. 3. Phototropin; photosynthetic efficiency optimized blue light receptor What is phototropin? Charles Darwin, who is famous for his theory of evolution, wrote in his book “The power of move-ment in plants” published in 1882 that plants bend toward blue light. Approximately 100 years later, the protein nph1 (nonphoto-tropic hypocotyl 1) encoded by one of the causative genes of Arabidopsis mutants causing phototropic abnormalities was identified as a blue photoreceptor. Later, another isotype npl1 was found and renamed phototropin 1 (phot1) and 2 (phot2), respectively. In addition to phototropism, phototropin is damaged by chloroplast photolocalization (chloroplasts move through the epidermal cells of the leaves and gather on the cell surface under appropriate light intensity for photosynthesis. As a photoreceptor for reactions such as escaping to the side of cells under dangerous strong light) and stomata (reactions that open stomata to optimize the uptake of carbon dioxide, which is the rate-determining process of photosynthetic reactions). It became clear that it worked. In this way, phototropin can be said to be a blue light receptor responsible for optimizing photosynthetic efficiency. Domain structure and LOV photoreaction of phototropin molecule Phototropin molecule has two photoreceptive domains (LOV1 and LOV2) called LOV (Light-Oxygen-Voltage sensing) on the N-terminal side, and serine / on the C-terminal side. It is a protein kinase that forms threonine kinase (STK) (Fig. 4Aa) and whose activity is regulated by light. LOV is one molecule as a chromophore, he binds FMN (flavin mononucleotide) non-covalently. The LOV forms an α/βfold, and the FMN is located on a β-sheet consisting of five antiparallel β-strands (Fig. 4B). The FMN in the ground state LOV shows the absorption spectrum of a typical oxidized flavin protein with a triplet oscillation structure and an absorption maximum wavelength of 450 nm, and is called D450 (Fig. 1C and Fig. 4E). After being excited to the singlet excited state by blue light, the FMN shifts to the triplet excited state (L660t *) due to intersystem crossing, and then the C4 (Fig. 4C) of the isoaroxazine ring of the FMN is conserved in the vicinity. It forms a transient accretionary prism with the tain (red part in Fig. 4B Eα) (S390I). When this cysteine is replaced with alanine (C / A substitution), the addition reaction does not occur. The effect of adduct formation propagates to the protein moiety, causing kinase activation (S390II). After that, the formed cysteine-flavin adduct spontaneously dissociates and returns to the original D450 (Fig. 4E, dark regression reaction). Phototropin kinase activity control mechanism by LOV2 Why does phototropin have two LOVs? Atphot1 was found as a protein that is rapidly autophosphorylated when irradiated with blue light. The effect of the above C / A substitution on this self-phosphorylation reaction and phototropism was investigated, and LOV2 is the main photomolecular switch in both self-phosphorylation and phototropism. It turns out that it functions as. After that, from experiments using artificial substrates, STK has a constitutive activity, LOV2 functions as an inhibitory domain of this activity, and the inhibition is eliminated by photoreaction, while LOV1 is kinase light. It was shown to modify the photosensitivity of the activation reaction. In addition to this, LOV1 was found to act as a dimerization site from the crystal structure and his SAXS. What kind of molecular mechanism does LOV2 use to photoregulate kinase activity? The following two modules play important roles in this intramolecular signal transduction. Figure 4 (A) Domain structure of LOV photoreceptors. a: Phototropin b: Neochrome c: FKF1 family protein d: Aureochrome (B) Crystal structure of auto barley phot1 LOV2. (C) Structure of FMN isoaroxazine ring. (D) Schematic diagram of the functional domain and module of Arabidopsis thaliana phot1. L, A’α, and Jα represent linker, A’α helix, and Jα helix, respectively. (E) LOV photoreaction. (F) Molecular structure model (mesh) of the LOV2-STK sample (black line) containing A’α of phot2 obtained based on SAXS under dark (top) and under bright (bottom). The yellow, red, and green space-filled models represent the crystal structures of LOV2-Jα, protein kinase A N-lobe, and C-robe, respectively, and black represents FMN. See the text for details. 1) Jα. LOV2 C of oat phot1-to α immediately after the terminus Rix (Jα) is present (Fig. 4D), which interacts with the β-sheet (Fig. 4B) that forms the FMN-bound scaffold of LOV2 in the dark, but unfolds and dissociates from the β-sheet with photoreaction. It was shown by NMR that it does. According to the crystal structure of LOV2-Jα, this Jα is located on the back surface of the β sheet and mainly has a hydrophobic interaction. The formation of S390II causes twisting of the isoaroxazine ring and protonation of N5 (Fig. 4C). As a result, the glutamine side chain present on his Iβ strand (Fig. 4B) in the β-sheet rotates to form a hydrogen bond with this protonated N5. Jα interacts with this his Iβ strand, and these changes are thought to cause the unfold-ing of Jα and dissociation from the β-sheet described above. Experiments such as amino acid substitution of Iβ strands revealed that kinases exhibit constitutive activity when this interaction is eliminated, and that Jα plays an important role in photoactivation of kinases. 2) A’α / Aβ gap. Recently, several results have been reported showing the involvement of amino acids near the A’α helix (Fig. 4D) located upstream of the N-terminal of LOV2 in kinase photoactivation. Therefore, he investigated the role of this A’α and its neighboring amino acids in kinase photoactivation, photoreaction, and Jα structural change for Atphot1. The LOV2-STK polypeptide (Fig. 4D, underlined in black) was used as a photocontrollable kinase for kinase activity analysis. As a result, it was found that the photoactivation of the kinase was abolished when amino acid substitution was introduced into the A’α / Aβ gap between A’α and Aβ of the LOV2 core. Interestingly, he had no effect on the structural changes in Jα examined on the peptide map due to the photoreaction of LOV2 or trypsin degradation. Therefore, the A’α / Aβ gap is considered to play an important role in intramolecular signal transduction after Jα. Structural changes detected by SAXS Structural changes of Jα have been detected by various biophysical methods other than NMR, but structural information on samples including up to STK is reported only by his results to his SAXS. Not. The SAXS measurement of the Atphot2 LOV2-STK polypeptide showed that the radius of inertia increased from 32.4 Å to 34.8 Å, and the molecular model (Fig. 4F) obtained by the ab initio modeling software GASBOR is that of LOV2 and STK. It was shown that the N lobes and C lobes lined up in tandem, and the relative position of LOV2 with respect to STK shifted by about 13 Å under light irradiation. The difference in the molecular model between the two is considered to reflect the structural changes that occur in the Jα and A’α / Aβ gaps mentioned above. Two phototropins with different photosensitivity In the phototropic reaction of Arabidopsis Arabidopsis, Arabidopsis responds to a very wide range of light intensities from 10–4 to 102 μmol photon / sec / m2. At that time, phot1 functions as an optical sensor in a wide range from low light to strong light, while phot2 reacts with light stronger than 1 μmol photon / sec / m2. What is the origin of these differences? As is well known, animal photoreceptors have a high photosensitivity due to the abundance of rhodopsin and the presence of biochemical amplification mechanisms. The exact abundance of phot1 and phot2 in vivo is unknown, but interesting results have been obtained in terms of amplification. The light intensity dependence of the photoactivation of the LOV2-STK polypeptide used in the above kinase analysis was investigated. It was found that phot1 was about 10 times more photosensitive than phot2. On the other hand, when the photochemical reactions of both were examined, it was found that the rate of the dark return reaction of phot1 was about 10 times slower than that of phot2. This result indicates that the longer the lifetime of S390II, which is in the kinase-activated state, the higher the photosensitivity of kinase activation. This correlation was further confirmed by extending the lifespan of her S390II with amino acid substitutions. This alone cannot explain the widespread differences in photosensitivity between phot1 and phot2, but it may explain some of them. Furthermore, it is necessary to investigate in detail protein modifications such as phosphorylation and the effects of phot interacting factors on photosensitivity. Other LOV photoreceptors Among fern plants and green algae, phytochrome ɾphotosensory module (PSM) on the N-terminal side and chimera photoreceptor with full-length phototropin on the C-terminal side, neochrome (Fig. There are types with 4Ab). It has been reported that some neochromes play a role in chloroplast photolocalization as a red light receiver. It is considered that fern plants have such a chimera photoreceptor in order to survive in a habitat such as undergrowth in a jungle where only red light reaches. In addition to this, plants have only one LOV domain, and three proteins involved in the degradation of photomorphogenesis-related proteins, FKF1 (Flavin-binding, Kelch repeat, F-box 1, ZTL (ZEITLUPE)), LKP2 ( There are LOV Kelch Protein2) (Fig. 4Ac) and aureochrome (Fig. 4Ad), which has a bZip domain on the N-terminal side of LOV and functions as a gene transcription factor. 4. Cryptochrome and UVR8 Cryptochrome is one of the blue photoreceptors and forms a superfamily with the DNA photoreceptor photolyase. It has FAD (flavin adenine dinucle-otide) as a chromophore and tetrahydrofolic acid, which is a condensing pigment. The ground state of FAD is considered to be the oxidized type, and the radical type (broken line in Fig. 1B) generated by blue light irradiation is considered to be the signaling state. The radical type also absorbs in the green to orange light region, and may widen the wavelength region of the plant morphogenesis reaction spectrum. Cryptochrome uses blue light to control physiological functions similar to phytochrome. It was identified as a photoreceptor from one of the causative genes of UVR8 Arabidopsis thaliana, and the chromophore is absorbed in the UVB region by a Trp triad consisting of three tryptophans (Fig. 1D). It is involved in the biosynthesis of flavonoids and anthocyanins that function as UV scavengers in plants. Conclusion It is thought that plants have acquired various photoreceptors necessary for their survival during a long evolutionary process. The photoreceptors that cover the existing far-red light to UVB mentioned here are considered to be some of them. More and more diverse photoreceptor genes are conserved in cyanobacteria and marine plankton. By examining these, it is thought that the understanding of plant photoreceptors will be further deepened.

Week 6 (27/02 - 05/03) During this week I will continue to feed the plants with Bio-grow, Bio-bloom and Top-max every other day. The two fat banana are in flowering stage by an entire week, while the blue cheese is in early stage of pre-flowering. The parameters remain unchanged with respect of the previous week: - light: 100% power, 18/6 h per day; - inkbird: 23.5°C, +1°C cooling, -3°C heating; - extractor: 50% power, 18h per day. 27/02 D35: removed a couple of lower leafs to the plants, they were a bit dry 28/02 D36: 1.5 liter of tap water each plant. Today I noticed some brown/orange spots on leaves of fat banana #1. Thanks to golden advises given to me by @GrowingGrannie, I will try to adjust nutrients in the next days. 01/03 D37: first day of recovery, sprayed leaves with tap water. 02/03 D38: second day of recovery, added 1.5ml of Bio-bloom and 1 ml of Top-max to 2.5 liters of tap water (almost 0.8 l each). 03/03 D39: third day of recovery, sprayed leaves with tap water. 04/03 D40: watering day. Added 2ml of Bio-bloom and 1ml of Top-Max to 2.5 liters of tap water. 05/03 D41: end of the week. The blue cheese has grown a lot this week reaching the taller fat banana #2. All three plants seem to be healthy.

Well week 5 of bloom is complete, and this week brought a few challenges. Humidity in my area has been through the roof, close to 100%. My heavy-duty equipment was struggling to bring my tent to acceptable late flowering levels, sometimes reaching over 60% RH, especially at night when the plant was respirating more. Additionally, her pale yellow color, and leathery leaves didn't excite me too much. If you remember, we had a severe heat wave a couple of weeks ago, which contributed to that. But also, since I messed up the ScrOG training, and regrettably decided not to super-crop her, a fair share of the leaf problems were due to light stress as well, as I didn't want to sacrifice lower colas, so I let it go. My biggest mistake this grow, was not paying attention to her the one day she decided to stretch nearly a foot, and was unable to be weaved into the net the next day without being snapped in half. My second biggest mistake is NOT snapping it in half, and letting it repair itself. I wouldn't have had nearly as much bleaching of leaves I think. This week, and I'm assuming because nearly all chlorophyll was depleted from her fan leaves, I didn't notice much of any change from last week. Her buds seemed to be about the same mass, and the stigmas still had the same ratio of red to white coloration. I suspected she was dead, or dying, or just...done. Not all genetics will transform all of their stigmas from white, and not all genetics will have their trichomes turn amber. So, I did a few things to confirm that suspicion. First, I looked at her trichomes on various buds closely with a microscope. They were almost all cloudy, with very very few amber. That told me that she was at an acceptable level of ripeness, even if she could have went longer, assuming she was still alive. Next, I removed the pea gravel mulch I was using in the raised bed, so I could get a closer look at the soil she was growing in, and more specifically, her roots. The soil, although moist a few inches deep, was not at the level I expected, and I think I have not been watering her enough. I don't think I'll be using a gravel mulch again. On the plus side, it did help prevent fungus gnats, as there was zero the whole grow, apart from an early week when I placed some solo cups to germinate on top of the bed, but after removing them, the fungus gnats disappeared with them. Also while inspecting the soil, I carefully dug down to inspect some of her primary roots. They were actually dry, despite the surrounding soil being moist. This could explain why she wasn't drinking much if any for the better part of the week. So, given her dry foliage, dry roots, and ripe-enough trichomes, I decided it was time to harvest her, earlier than expected. Let's also not forget that I was frightened this week with some high humidity scares, so growing longer, and possibly for no reason if she was dead or barely alive, was not in the cards. I've dealt with my fair share of bud rot before, and I would rather try what I have of her now, than to wait the extra week or so for her to be fully ripe. So, that is what I did, on the last day of the week -- I chopped her down, cut off some larger fan leaves, and hung her upside down. This, of course, was after removing the raised bed. It took me a while to empty about 45 gallons of soil so I could move it, but in doing so, I noticed a lot of beneficial critters, and nothing bad. Such critters included small centipedes, which feed on other insects, and soil mites which eat dead organic matter. I set the tent to dry at around 72F and 55 RH. And now we wait for about a week before trimming. One thing is for sure -- I am very proud of this grow, despite all these flaws. She smells incredible -- like pure citrus emanating throughout my house. This is a very strong-smelling plant. As a bonus, I've included a time-lapse video of the entire grow from start to finish in the last media above. Check it out and let me know what you think. I'll be back for the harvest week for the dry weight in about a week or so, after we're done drying and trimming.

Week 5 and I expected the flowering begins soon. But it's around the corner for sure!

Week 3 Watered Plants Ph Water 6 Used 2.5 Ml Of Recharge Still Using Living Soil 18/6 Hour Light INTRODUCE LST TO PLANT Noticed Plants Growing At Different Rates Idk Why All Sprouted Same Day Weird

Day 71 Update: Watered both plants with almost a gallon until runoff. Water was just plain pH balanced water. Plant #1 has 5 days left on flush and Plant #2 has 11 days left on flush. Although with my tent filling up, I will probably harvest Plant #1 tomorrow as I don't think 4 days of being in there will make a difference in the end product. Day 72 Update: Harvested Plant #1 today. Plant #2 has 10 days left on flush. Day 74 Update: Watered plant with 3/4gal of pH balanced water until runoff. Plant #2 has 8 days left on flush. Also, added another stake to help support a heavier branch. Day 76 Update: Placed buds from Plant #1 in jars to start curing...maybe a little bit too long drying, but if that's the case I'll toss a boveda pack in. Plant #1's yield was 57.2g or 2oz 1.2g. Plant #2 will be harvested sometime next week and I will update the harvest page as soon as buds are dried and weighed.

Day 36 (Bettis). Just starting to flower. Doing some minor defoliation and supercropping. Very satisfied with her progress. Day 41. Continuing with minor defoliation and supercropping.

Buenas a tod@s... Segunda semana de floracion de las tropicanna poison de sweet seed, la variedad se la ve bien, fuerte, los nutrientes son muy buenos, aún q es mi segundo armario ya se va notando un gran cambio, espero q siga todo bien, se que si... 💪🏻💪🏻 A seguir trabajando... Buenos humos para tod@s.. 💨💨💨🔥🔥 😎💎 🇦🇷🤝🏻🇪🇦

Going to extend 1, possibly 2 more weeks of veg; want to manifold and fill out the table more before flipping to flower. Defoliation, tucking, LST

Unfortunately these ladies had to be cut earlier before finish as im moving abroad and plans happened alot quicker then I was expecting,anyway very strong genetics from FastBuds I will be back very soon with some autodoors grows Will upload the last photos of their life once again amazing genetics