1VFR
THE MAJOR NAD(P)H:FMN OXIDOREDUCTASE FROM VIBRIO FISCHERI
Experimental procedure
Source type | SYNCHROTRON |
Source details | PHOTON FACTORY BEAMLINE BL-6B |
Synchrotron site | Photon Factory |
Beamline | BL-6B |
Temperature [K] | 285 |
Detector technology | IMAGE PLATE |
Collection date | 1995-04 |
Detector | FUJI |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 101.600, 63.300, 74.400 |
Unit cell angles | 90.00, 100.00, 90.00 |
Refinement procedure
Resolution | 10.000 - 1.800 |
R-factor | 0.187 |
Rwork | 0.187 |
R-free | 0.21300 |
Structure solution method | MULTIPLE ISOMORPHOUS REPLACEMENT |
RMSD bond length | 0.010 |
RMSD bond angle | 22.830 * |
Data reduction software | WEIS |
Data scaling software | CCP4 |
Phasing software | X-PLOR (3.1) |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 1.880 | |
High resolution limit [Å] | 1.800 | 1.790 |
Rmerge | 0.059 | 0.297 |
Total number of observations | 180543 * | |
Number of reflections | 39895 * | |
<I/σ(I)> | 2.6 | |
Completeness [%] | 91.3 | 74.4 |
Redundancy | 3.3 | 3.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 8.5 | 25 * | pH 8.5 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 20 (mg/ml) | |
2 | 1 | reservoir | PEG4000 | 30 (%(w/v)) | |
3 | 1 | reservoir | sodium acetate | 0.2 (M) | |
4 | 1 | reservoir | FMN | 0.1 (mM) | |
5 | 1 | reservoir | Tris-HCl | 100 (mM) |