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purified His-tagged wild-type and mutant H171C enzymes, hanging drop vapor diffusion method, 0.002 ml of 10 mg/ml protein in 20 mM Tris-HCl, pH 8.5, with 1 mM fructose 1,6-bisphosphate and NAD+, is mixed with 0.002 ml of reservoir solution containing 16% w/v PEG MME 2000, 0.06 M sodium/potassium phosphate, 1.8% v/v glycerol pH 5.5, or 14% w/v PEG 4000, 0.1 M sodium/potassium phosphate, 2% v/v glycerol, pH 7.0, equilibration against 1 ml reservoir solution, X-ray diffraction structure determinaation and analysis at 2.2-2.5 A resolution
purified enzyme, hanging drop vapor diffusion technique, 8 mg/ml protein in 20% PEG 5000 MME, 0.1M bicine, pH 9.0, at room temperature, X-ray diffraction structure determination and analysis at 2.5 A resolution, molecular replacement
binary complex of LDH with the cofactor NADH and the LDH/NADH-oxamate ternary complex, molecular dynamics, and simulation model from crystal structure at 2.1 A resolution, Protein DataBank entry 1IOZ, overview
crystals the apo-form of PfLDH are ontained by hanging-drop method with 2-methyl-2,4-pentanediol as precipitant, crystallization of enzyme:naphthoic acid complexes with 2,6-naphthalenedicarboxalic acid, 2,6-naphthalene disulfonic acid or 3,7-dihydroxy naphthalene-2-carboxylic acid and 3,7-dihydroxy naphthalene-2-carboxylic acid plus NAD+
purified recombinant His-tagged Sa-LDH-1, sitting drop vapour diffusion method, 0.001 ml protein solution, containing 5 mg/ml protein in 20 mM Tris-HCl, 200 mM NaCl, pH 7.5, is mixed with mixed with an equal volume of reservoir solution, containing ,0.2 M calcium chloride dihydrate, 0.1 M Na HEPES, pH 7.5, 28%(v/v) PEG 400, and equilibrated against 0.1 ml reservoir solution, 3 days, X-ray diffraction structure determination and analysis at 2.4 A resolution