2WP9
Crystal structure of the E. coli succinate:quinone oxidoreductase (SQR) SdhB His207Thr mutant
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID23-1 |
Synchrotron site | ESRF |
Beamline | ID23-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2008-07-24 |
Detector | ADSC CCD |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 119.853, 183.803, 202.777 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 48.850 - 2.700 |
R-factor | 0.19192 |
Rwork | 0.190 |
R-free | 0.22247 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2wdq |
RMSD bond length | 0.012 |
RMSD bond angle | 1.357 |
Data reduction software | XDS |
Data scaling software | SCALA |
Phasing software | REFMAC |
Refinement software | REFMAC (5.4.0067) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 49.630 | 2.850 |
High resolution limit [Å] | 2.700 | 2.700 |
Rmerge | 0.090 | 0.640 |
Number of reflections | 122882 | |
<I/σ(I)> | 11.1 | 2 |
Completeness [%] | 99.9 | 100 |
Redundancy | 3.7 | 3.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 8.5 | 0.1M TRIS PH 8.5, 0.1M LI2SO4, 0.1M NACL, 0.009% DDM, 3% 1,6-HEXANEDIOL AND 10% (W/V) PEG4000 |