EC Number   |
|---|
   1.6.2.2 | fully reduced form and the oxidized form of the purified liver enzyme, X-ray diffraction structure determination and analysis at 1.68 A resolution |
| 1.6.2.2 | hanging drop vapor diffusion method, using 9-12% (w/v) PEG 4,000, 100 mM potassium phosphate (pH 7.7) and 5 mM dithiothreitol |
| 1.6.2.2 | hanging-drop vapour-diffusion method |
| 1.6.2.2 | sitting drop method |
| 1.6.2.2 | sitting drop method, complete data set collected for the D239T mutant enzyme |
| 1.6.2.2 | sitting drop method, reservoir: 8% poly ethylene glycol 6000, 5% 2-methyl-2,4-pentanediol in 100 mM 4-(2-hydroxyethyl)piperazine-1-ethanesulfonic acid, pH 7.5, X-ray structure, resolution: enzyme 2.0 A, enzyme-NAD+ complex, 2.3 A |
| 1.6.2.2 | sitting drop vapor diffusion method, using 2 M (NH4)2SO4, 100 mM sodium/potassium phosphate, pH 6.2, 200 mM Li2SO4, at 4°C |
| 1.6.2.2 | sitting-drop vapor diffusion method |
| 1.6.2.2 | structure of a construct comprising the naturally fused CHORD-Sgt1 and b5R domains with bound FAD and NAD+ or NADP+. The linker between the CHORD-Sgt1 and b5R cores is more ordered than predicted, with much of it extending the beta-sandwich motif of the CHORD-Sgt1 domain. This limits the flexibility between the two domains |
| 1.6.2.2 | structure of the cytochrome b5 reductase domain. The N-terminal FAD-binding domain primarily consists of six antiparallel beta-strands, a C-terminal NADH-binding domain forming a Rossmann fold, and a three beta-stranded linker region connecting these two domains. The FAD cofactor is located in the cleft between the two domains and interacts primarily with the FAD-binding domain |
