3U0G
Crystal structure of branched-chain amino acid aminotransferase from burkholderia pseudomallei
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 5.0.3 |
Synchrotron site | ALS |
Beamline | 5.0.3 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-12-19 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.97650 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 106.970, 139.270, 290.860 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 1.900 |
R-factor | 0.1936 |
Rwork | 0.192 |
R-free | 0.22964 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1wrv |
RMSD bond length | 0.015 |
RMSD bond angle | 1.762 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 20.000 |
High resolution limit [Å] | 1.900 |
Rmerge | 0.076 |
Number of reflections | 126128 |
Completeness [%] | 99.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 9.5 | 293 | 20% PEG 8000, 100MM CHES, PROTEIN CONCENTRATION 23.1 MG/ML, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K, pH 9.50 |