3M1G
The structure of a putative glutathione S-transferase from Corynebacterium glutamicum
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-02-16 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.97948, 0.97935 |
Spacegroup name | I 4 2 2 |
Unit cell lengths | 167.245, 167.245, 226.855 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 45.450 - 2.100 |
R-factor | 0.152 |
Rwork | 0.151 |
R-free | 0.17600 |
Structure solution method | MAD |
RMSD bond length | 0.017 |
RMSD bond angle | 1.448 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | MLPHARE |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.140 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.079 | 0.667 |
Number of reflections | 92656 | |
<I/σ(I)> | 8.4 | |
Completeness [%] | 99.9 | 100 |
Redundancy | 11 | 11.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.4 | 278 | 0.2M sodium potassium tartrate, 20% PEG 3350, trypsin in situ, pH 7.4, VAPOR DIFFUSION, SITTING DROP, temperature 278K |