3HUD
THE STRUCTURE OF HUMAN BETA 1 BETA 1 ALCOHOL DEHYDROGENASE: CATALYTIC EFFECTS OF NON-ACTIVE-SITE SUBSTITUTIONS
Experimental procedure
| Spacegroup name | P 1 |
| Unit cell lengths | 54.590, 45.050, 93.860 |
| Unit cell angles | 91.93, 102.50, 68.82 |
Refinement procedure
| Resolution | 8.000 - 3.200 |
| R-factor | 0.179 |
| Rwork | 0.179 |
| RMSD bond length | 0.015 |
| RMSD bond angle | 3.560 |
| Phasing software | X-PLOR |
| Refinement software | X-PLOR |
Data quality characteristics
| Overall | |
| High resolution limit [Å] | 2.880 * |
| Rmerge | 0.060 * |
| Number of reflections | 11114 * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | sodium phosphate | 50 (mM) | |
| 2 | 1 | reservoir | NAD+ | 1 (mM) | |
| 3 | 1 | reservoir | PEG8000 | 12.5 (%(w/v)) | |
| 4 | 1 | drop | protein | 10-15 (mg/ml) |
