1ROM
CRYSTAL STRUCTURE OF NITRIC REDUCTASE FROM DENITRIFYING FUNGUS FUSARIUM OXYSPORUM
Experimental procedure
Source type | SYNCHROTRON |
Source details | PHOTON FACTORY BEAMLINE BL-6A |
Synchrotron site | Photon Factory |
Beamline | BL-6A |
Temperature [K] | 288 |
Detector technology | IMAGE PLATE |
Collection date | 1995-12-10 |
Detector | FUJI |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 54.990, 82.660, 87.210 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 10.000 - 2.000 |
R-factor | 0.197 |
Rwork | 0.197 |
R-free | 0.26600 |
Structure solution method | MIR |
RMSD bond length | 0.007 |
RMSD bond angle | 22.800 * |
Data reduction software | DENZO |
Data scaling software | CCP4 ((SCALA) |
Phasing software | X-PLOR (3.851) |
Refinement software | X-PLOR (3.851) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 100.000 | 2.240 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.054 | 0.107 |
Total number of observations | 84152 * | |
Number of reflections | 24733 | |
<I/σ(I)> | 9.9 | 7 |
Completeness [%] | 90.1 | 79.5 |
Redundancy | 3.4 | 2.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, sitting drop * | 5.5 | Park, S.Y., (1997) FEBS Lett. 412, 346. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | MES | 100 (mM) | |
2 | 1 | drop | protein | 25 (mg/ml) | |
3 | 1 | drop | MES | 50 (mM) | |
4 | 1 | reservoir | PEG4000 | ||
5 | 1 | drop | PEG4000 |