3E03
Crystal structure of a putative dehydrogenase from Xanthomonas campestris
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 31-ID |
Synchrotron site | APS |
Beamline | 31-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2008-06-26 |
Detector | MAR CCD 165 mm |
Wavelength(s) | 0.97929 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 251.286, 41.351, 73.323 |
Unit cell angles | 90.00, 96.62, 90.00 |
Refinement procedure
Resolution | 19.630 - 1.690 |
R-factor | 0.162 |
Rwork | 0.161 |
R-free | 0.19900 |
RMSD bond length | 0.013 |
RMSD bond angle | 1.306 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | SHELXS |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 44.770 | 1.780 |
High resolution limit [Å] | 1.690 | 1.690 |
Number of reflections | 83754 | |
<I/σ(I)> | 7.4 | 3.4 |
Completeness [%] | 99.9 | 99.9 |
Redundancy | 7 | 7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 294 | 100mM HEPES pH 7.5, 0.2M Calciumchloride,10% PEG 8000, VAPOR DIFFUSION, SITTING DROP, temperature 294K |