3GMS
Crystal structure of putative NADPH:quinone reductase from bacillus thuringiensis
Experimental procedure
Experimental method | SAD |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X29A |
Synchrotron site | NSLS |
Beamline | X29A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2008-12-09 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.979 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 68.599, 94.772, 67.573 |
Unit cell angles | 90.00, 112.97, 90.00 |
Refinement procedure
Resolution | 50.000 - 1.760 |
R-factor | 0.2 |
Rwork | 0.199 |
R-free | 0.23400 |
Structure solution method | SAD |
RMSD bond length | 0.015 |
RMSD bond angle | 1.447 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SHELXD |
Refinement software | REFMAC |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 1.820 |
High resolution limit [Å] | 1.760 | 3.790 | 1.760 |
Rmerge | 0.069 | 0.051 | 0.367 |
Number of reflections | 76483 | ||
<I/σ(I)> | 17.826 | ||
Completeness [%] | 98.3 | 93.1 | 95.5 |
Redundancy | 3.1 | 2.9 | 2.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 298 | 0.1M Sodium Hepes pH 7.5, 30% PEG 400, 0.2M MgCl2, VAPOR DIFFUSION, SITTING DROP, temperature 298K |