1YBV
STRUCTURE OF TRIHYDROXYNAPHTHALENE REDUCTASE IN COMPLEX WITH NADPH AND AN ACTIVE SITE INHIBITOR
Experimental procedure
| Detector technology | IMAGE PLATE |
| Collection date | 1994-12-16 |
| Detector | RIGAKU RAXIS |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 142.600, 142.600, 72.900 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 8.000 - 2.800 |
| R-factor | 0.223 |
| Rwork | 0.223 |
| R-free | 0.25400 |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.500 |
| Data reduction software | DENZO |
| Phasing software | X-PLOR |
| Refinement software | X-PLOR |
Data quality characteristics
| Overall | |
| High resolution limit [Å] | 2.800 * |
| Rmerge | 0.086 |
| Total number of observations | 111124 * |
| Number of reflections | 19294 |
| Completeness [%] | 91.4 |
| Redundancy | 5.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | Andersson, A., (1996) Proteins: Struct.,Funct., Genet., 24, 525. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | drop | HEPES | 2.5 (mM) | |
| 3 | 1 | drop | 2.5 (mM) | ||
| 4 | 1 | drop | PEG6000 | 9 (%) | |
| 5 | 1 | reservoir | PEG6000 | 18 (%) |
