4YQV
Glutathione S-transferase Omega 1 bound to covalent inhibitor C4-10
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-D |
Synchrotron site | APS |
Beamline | 21-ID-D |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2012-10-11 |
Detector | RAYONIX MX-300 |
Wavelength(s) | 0.9786 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 186.320, 71.373, 61.968 |
Unit cell angles | 90.00, 105.16, 90.00 |
Refinement procedure
Resolution | 44.960 - 2.060 |
R-factor | 0.196 |
Rwork | 0.195 |
R-free | 0.22000 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1eem |
RMSD bond length | 0.009 |
RMSD bond angle | 0.920 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | BUSTER (2.10.2) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.140 |
High resolution limit [Å] | 2.060 | 2.060 |
Rmerge | 0.078 | 0.316 |
Number of reflections | 46437 | |
<I/σ(I)> | 11.2 | |
Completeness [%] | 98.0 | 99.3 |
Redundancy | 5 | 4.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293 | Complex was concentrated to 26.2 mg/mL. Crystals of the complex grew from sitting drops containing equal volumes of protein complex and well solution (22.5% PEG 3350, 90 mM MES pH 6.5 and 10 mM BaCl2). |