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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
5 mg/ml purified native enzyme with FMN bound in 100 mM K2PO4, pH 7.5, and 5 mM 2-mercaptoethanol, mixed with an equal volume of reservoir solution containing 60 mM HEPES, pH 6.8, and 0.65 M KH2PO4/NH4H2PO4, formation of tetragonal crystals within 4-5 weeks, X-ray diffraction structure determination and analysis at 2.6 A resolution, molecular-replacement method
hanging-drop and sitting-drop method, crystallized without and with an excess of pyridoxal 5'-phosphate. Structures are determined to 1.95 A and 2.65 A, respectively
purified recombinant enzyme from strain Rv1155, sitting drop vapour diffusion method, 9 mg/ml enzyme in 50 mM Tris-HCl, pH 8.0, 25-50 mM KF, and 10 mM glutathione, mixed with an equal volume of precipitation solution containing 0.1 M HEPES, pH 7.5, 8% ethylene glycol, and 10% PEG 8000, macroseeding with hanging drops containing equal volumes of protein and precipitation solutions overnight prior to seeding, 1-2 weeks, cryoprotection by 30% ethylene glycol, X-ray diffraction structure determination and analysis at 1.7-2.2 A, modeling
purified recombinant enzyme from strain Rv2074, sitting drop vapour diffusion method in microtiter plates at room temperature, 12 mg/ml enzyme in 50 mM Tris-HCl, pH 8.0, 5 mM DTT, and glutathione, mixed with an equal volume of precipitation solution containing 0.2 M sodium citrate, pH 5.0, 30% glycerol, and 20% PEG 4000, hanging drop vapour diffusion with 0.5 ml protein and 1 ml precipitation solutions mixed, 1-2 weeks, cryoprotection by 30% glycerol, X-ray diffraction structure determination and analysis at 2.0 A, modeling