Crystallization and preliminary X-ray studies on the molbindin ModG from Azotobacter vinelandii
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Abstract:
Crystals of the molbindin ModG (subunit M r = 14359 Da), a cytoplasmic molybdate-binding protein from Azotobacter vinelandii , were grown by vapour diffusion. Both apo and tungstate-bound forms were crystallized and X-ray data were collected at 100 K. Apo-ModG crystallizes in space group P 6 3 22, with unit-cell dimensions a = b = 90.62, c = 79.46 Å. Native data to a resolution of 2.5 Å were collected from a single crystal, which showed a marked improvement in diffraction quality after annealing. Data from a single-site gold derivative were also collected at 2.7 Å resolution. Crystals of the ligand-bound form of ModG belong to space group P 321, with unit-cell parameters a = b = 50.57, c = 79.29 Å. X-ray data to a resolution of 2.0 Å were collected.Keywords:
Azotobacter vinelandii
Azotobacter vinelandii
Azotobacter
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Isolation and identification and primary application of Azotobacter vinelandii were studied.The results showed that through isolation,culture and identification,6 strains of Azotobacter vinelandii were obtained.Among them,four strains had certain nitrogen fixation ability,and other two strains were even better.Using Azotobacter vinelandii,the bacterial fertilizer was made,and it significantly increased the yield of ryegrass.
Azotobacter vinelandii
Azotobacter
Isolation
Azotobacteraceae
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Azotobacter vinelandii
Hydrogenase
Azotobacteraceae
Methylene blue
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آلژینات پلیمر پلی ساکاریدی متشکل از زیر واحدهای ? D- مانورونات و ? L-گولورونات است که کاربردهای متعددی دارد. اگرچه تا به امروز این ترکیبات از منابع جلبکی استخراج شده، ولی اخیرا آلژینات باکتریایی به عنوان محصول تجاری مورد توجه قرار گرفته است. در این تحقیق 100 نمونه خاک کشاورزی برای جداسازی Azotobacter vinelandii، مهمترین باکتری مولد آلژینات از نظر بیوتکنولوژی، کشت شد. برای افزایش احتمال جداسازی A. vinelandii روشهایی نیز به کار گرفته شد که شامل فقدان هر گونه منبع نیتروژن در محیط کشت ، افزودن % 1/0 فنل، استفاده از اتیلن گلیگول به عنوان تنها منبع کربن محیط و انکوباسیون در o C 37 بود. با آزمایشهای مرفولوژیک و بیو‌شیمیایی بر 18 سویه مولد اگزوپلیمر جدا شده، 14 سویه A. vinelandii و
4 سویه A. chroococcum شناخته شد. همه این سویه ها در محیط کشت دارای منبع کربن سوکروز، در oC30، rpm180 به مدت 96 ساعت انکوباسیون شد. پس از جداسازی بیوماس، پلیمر استخراج و غلظت آن اندازه‌گیری شد. در بین 18 سویه مولد آلژینات، A.vinelandii UT15 بیشترین بازده را داشته است (g/l5/1) و تاثیر عوامل محیطی pH، درجه حرارت، سرعت همزن و غلظت و نوع منبع کربن بر تولید آلژینات با این سویه بررسی شده است. نتایج حاصل نشان می‌دهد که بهترین شرایط برای تولید آلژینات pH 7، درجه حرارت oC34، rpm 180 و غلظت g/l20 سوکروز بوده است. در این شرایط A.vinelandii UT15 g/l73/1 آلژینات تولید کرده است.
Azotobacter vinelandii
Azotobacteraceae
Azotobacter chroococcum
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Azotobacter vinelandii
Azotobacter
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Azotobacter vinelandii (A. vinelandii) is a commonly used model organism for the study of aerobic respiration, the bacterial production of several industrially relevant compounds, and, perhaps most significantly, the genetics and biochemistry of biological nitrogen fixation. Laboratory growth assessments of A. vinelandii are useful for evaluating the impact of environmental and genetic modifications on physiological properties, including diazotrophy. However, researchers typically rely on manual growth methods that are oftentimes laborious and inefficient. We present a protocol for the automated growth assessment of A. vinelandii on a microplate reader, particularly well-suited for studies of diazotrophic growth. We discuss common pitfalls and strategies for protocol optimization, and demonstrate the protocol's application toward growth evaluation of strains carrying modifications to nitrogen-fixation genes. © 2021 The Authors. Basic Protocol 1: Preparation of A. vinelandii plate cultures from frozen stock Basic Protocol 2: Preparation of A. vinelandii liquid precultures Basic Protocol 3: Automated growth rate experiment of A. vinelandii on a microplate reader.
Azotobacter vinelandii
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Azotobacter vinelandii
Azotobacter
Azotobacteraceae
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Azotobacter vinelandii
Azotobacter
Azotobacteraceae
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Azotobacter vinelandii
Azotobacter
Azotobacteraceae
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Preliminary x-ray diffraction data from single crystals of the MoFe proteins of nitrogenase from Clostridium pasteurianum and Azotobacter vinelandii have been obtained. Both protein crystals belong to the P2(1) space group. The MoFe protein crystals from C. pasteurianum and A. vinelandii diffract to angles corresponding to resolutions as great as 2.4 A and 3.0 A, respectively. The cell dimensions of the MoFe protein crystals from the two species have been determined from precession photographs.
Azotobacter vinelandii
Azotobacter
Azotobacteraceae
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