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 (%) |