2VOC
THIOREDOXIN A ACTIVE SITE MUTANTS FORM MIXED DISULFIDE DIMERS THAT RESEMBLE ENZYME-SUBSTRATE REACTION INTERMEDIATE
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM14 |
Synchrotron site | ESRF |
Beamline | BM14 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-03-10 |
Detector | MARRESEARCH |
Spacegroup name | P 1 |
Unit cell lengths | 36.765, 38.395, 41.878 |
Unit cell angles | 83.33, 66.62, 78.08 |
Refinement procedure
Resolution | 22.950 - 1.500 |
R-factor | 0.188 |
Rwork | 0.185 |
R-free | 0.23700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | POLYSERINE MODEL OF PDB ENTRY 2TRX |
RMSD bond length | 0.021 |
RMSD bond angle | 2.048 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.550 |
High resolution limit [Å] | 1.500 | 1.500 |
Rmerge | 0.070 | 0.340 |
Number of reflections | 31147 | |
<I/σ(I)> | 15.6 | 1.9 |
Completeness [%] | 94.5 | 90.1 |
Redundancy | 2.8 | 2.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7.8 | 0.1 M TRIS PH 7.8, 0.1 M MAGNESIUM CHLORIDE, 4% ACETONITRILE, 35% PEG 4000 |