2I0Z
Crystal structure of a FAD binding protein from Bacillus cereus, a putative NAD(FAD)-utilizing dehydrogenases
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 23-ID-D |
Synchrotron site | APS |
Beamline | 23-ID-D |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-03-06 |
Detector | MARRESEARCH |
Wavelength(s) | 0.98400 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 46.716, 92.366, 97.504 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 24.860 - 1.840 |
R-factor | 0.19779 |
Rwork | 0.195 |
R-free | 0.24794 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2gqf |
RMSD bond length | 0.012 |
RMSD bond angle | 1.329 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.000 | 1.920 |
High resolution limit [Å] | 1.840 | 1.840 |
Rmerge | 0.075 | 0.394 |
Number of reflections | 36967 | |
<I/σ(I)> | 13.9 | 3.9 |
Completeness [%] | 98.9 | 99.7 |
Redundancy | 3.9 | 3.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.3 | 295 | 0.01M TRIS-HCL, 0.2M Ammonium chloride, 0.25M Sodium chloride, 20% PEG 3350, pH 8.3, VAPOR DIFFUSION, SITTING DROP, temperature 295K |