2XR0
Room temperature X-ray structure of the perdeuterated Toho-1 R274N R276N double mutant beta-lactamase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 22-ID |
Synchrotron site | APS |
Beamline | 22-ID |
Temperature [K] | 293 |
Detector technology | CCD |
Collection date | 2010-04-04 |
Detector | MARRESEARCH MX-300 |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 73.500, 73.500, 99.330 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 29.540 - 2.200 |
R-factor | 0.135 |
Rwork | 0.133 |
R-free | 0.17300 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2wyx |
RMSD bond length | 0.009 |
RMSD bond angle | 1.122 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | PHENIX ((PHENIX.REFINE: 1.6.4_486)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 29.540 | 2.320 |
High resolution limit [Å] | 2.200 | 2.200 |
Rmerge | 0.050 | 0.830 |
Number of reflections | 15962 | |
<I/σ(I)> | 31.3 | 22 |
Completeness [%] | 98.6 | 97.9 |
Redundancy | 7.5 | 7.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 6.5 | 2.0 A AMMONIUM SULFATE, 0.1 M SODIUM CITRATE, PD 5.1. PREPARED IN 99.9% D2O AND MIXED 1:1 WITH PERDEUTERATED PROTEIN PREPARED IN 20 MM NA MES AT PD 6.1 (PH 6.5). |