4YQU
Glutathione S-transferase Omega 1 bound to covalent inhibitor C1-31
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-G |
Synchrotron site | APS |
Beamline | 21-ID-G |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2012-10-11 |
Detector | RAYONIX MX-300 |
Wavelength(s) | 0.9786 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 62.645, 72.588, 65.310 |
Unit cell angles | 90.00, 112.69, 90.00 |
Refinement procedure
Resolution | 45.220 - 1.940 |
R-factor | 0.2049 |
Rwork | 0.203 |
R-free | 0.24030 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1eem |
RMSD bond length | 0.010 |
RMSD bond angle | 0.940 |
Data scaling software | HKL-2000 |
Refinement software | BUSTER-TNT (BUSTER 2.11.2) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 1.970 |
High resolution limit [Å] | 1.940 | 5.260 | 1.940 |
Rmerge | 0.074 | 0.063 | 0.343 |
Total number of observations | 114158 | ||
Number of reflections | 36745 | ||
<I/σ(I)> | 16 | ||
Completeness [%] | 93.4 | 93.6 | 97.5 |
Redundancy | 3.1 | 3.2 | 2.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293 | The GSTO1-C1-31 complex was concentrated to 23.9 mg/mL prior to crystallization. Crystals formed from drops containing equal volumes of complex and well solution (22.5% PEG 3350, 90 mM MES pH 6.5 and 4% tert-butanol). |