2YKV
Structural Determinants of the Beta-Selectivity of a Bacterial Aminotransferase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-1 |
Synchrotron site | ESRF |
Beamline | ID14-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-09-25 |
Detector | ADSC CCD |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 183.582, 94.321, 102.307 |
Unit cell angles | 90.00, 113.99, 90.00 |
Refinement procedure
Resolution | 48.090 - 1.900 |
R-factor | 0.17737 |
Rwork | 0.176 |
R-free | 0.20603 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | MES_BFAT_APO |
RMSD bond length | 0.012 |
RMSD bond angle | 1.252 |
Data reduction software | XDS |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 48.090 | 2.000 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.070 | 0.380 |
Number of reflections | 125289 | |
<I/σ(I)> | 11.9 | 2.8 |
Completeness [%] | 99.9 | 100 |
Redundancy | 3 | 2.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | SAME AS WILD-TYPE APO |