4F0C
Crystal structure of the glutathione transferase URE2P5 from Phanerochaete chrysosporium
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM30A |
Synchrotron site | ESRF |
Beamline | BM30A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2011-11-04 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.97993 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 73.101, 73.101, 97.105 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 31.654 - 1.901 |
R-factor | 0.1422 |
Rwork | 0.141 |
R-free | 0.16900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4f0b |
RMSD bond length | 0.013 |
RMSD bond angle | 1.296 |
Data reduction software | XDS |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | PHENIX ((phenix.refine: 1.7.3_928)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 48.550 | 2.000 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.057 | 0.180 |
Number of reflections | 23921 | |
<I/σ(I)> | 11.9 | 4.1 |
Completeness [%] | 99.3 | 99.3 |
Redundancy | 2.9 | 2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7.7 | 277 | 3.5M Ammonium Sulfate, pH 7.7, MICROBATCH, temperature 277K |