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Results 1 - 10 of 17 > >>
EC Number Crystallization (Commentary)
Show all pathways known for 1.1.1.27Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.27-
Show all pathways known for 1.1.1.27Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.272.1 A resolution as a quarternary complex with the cofactor NADH, the allosteric activator fructose-1,6-bisphosphate and the substrate analog oxamate
Show all pathways known for 1.1.1.27Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.27apo enzyme form and enzyme in ternary complex, X-ray diffraction structure determination and analysis at 2.1-2.3 A resolution, molecular replacement
Show all pathways known for 1.1.1.27Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.27apo enzyme form, X-ray diffraction structure determination and analysis at 2.35 A resolution, molecular replacement
Show all pathways known for 1.1.1.27Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.27binary 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
Show all pathways known for 1.1.1.27Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.27crystal structure of a mutant into which an additional loop has been engineered in order to prevent tetramerization
Show all pathways known for 1.1.1.27Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.27crystals 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+
Show all pathways known for 1.1.1.27Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.27hanging drop method of vapour diffusion, ternary complex with NADH and oxamate
Show all pathways known for 1.1.1.27Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.27in apo-form and in ternary complexes containing NAD+ or NAD+-analogue 3-acetylpyridine adenine dinucleotide and sulfate or the inhibitor oxalate
Show all pathways known for 1.1.1.27Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.27lactate dehydrogenase A in apo form, in ternary complex with oxalate and kanamycin, and in inhibitor-bound form, hanging drop vapour diffusion method, apo-LDHA crystals are grown by mixing of 0.002 ml of 25 mg/ml enzyme protein with 0.002 ml reservoir solution consisting of 100 mM Bis-Tris propane, pH 7.0, 20% v/v PEG 400, and 100 mM LiCl. LDHA-NADH crystals are grown by first incubating 25 mg/ml enzyme protein with 3 mM NADH for 2 h at 4°C and then setting up 0.004 ml drops with a 2:1:1 volume ratio of LDHA-NADH, reservoir solution, containing 18% w/v PEG 3350, and 50 mM HEPES, pH 6.8, and another reagent containing 0.16% w/v L-citrulline, 0.16% w/v L-ornithine hydrochloride, 0.16% w/v urea, 0.16% w/v oxalic acid, 0.16% w/v kanamycin monosulfate, and 0.16% w/v L-arginine in 0.02 M HEPES sodium, pH 6.8, 20°C. Apo and NADH-bound LDHA crystals appear after three weeks. LDHA-inhibitor complex crystals are obtained by adding 0.010 ml soaking solution containing 20 mM inhibitor, 100 mM HEPES, pH 7.5, 50 mM LiCl, 100 mM bis-tris propane pH 7.0, 20% v/v DMSO, and 25% PEG 8000, to 0.002 ml hanging drops containing apo LDHA crystals and allowing the crystals to sit at room temperature for 24 h, X-ray diffraction structure determination and analysis at 2.1-3.2 A resolution, molecular replacement method using model structure PDB ID1i10
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