2YKU
Structural Determinants of the Beta-Selectivity of a Bacterial Aminotransferase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-2 |
Synchrotron site | ESRF |
Beamline | ID14-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-07-27 |
Detector | ADSC CCD |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 184.195, 94.833, 104.892 |
Unit cell angles | 90.00, 113.72, 90.00 |
Refinement procedure
Resolution | 96.030 - 1.900 |
R-factor | 0.16364 |
Rwork | 0.162 |
R-free | 0.19099 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | PDB ENTRIES 2E7U 2cy8 1ohv |
RMSD bond length | 0.010 |
RMSD bond angle | 1.252 |
Data reduction software | XDS |
Data scaling software | SCALA |
Phasing software | PHASER (FOR MR) |
Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 48.350 | 2.000 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.060 | 0.330 |
Number of reflections | 129742 | |
<I/σ(I)> | 12.6 | 3.2 |
Completeness [%] | 99.9 | 99.8 |
Redundancy | 2.6 | 2.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 0.1 M HEPES PH 7.5, 8% V/V ETHYLENE GLYCOL, 10 % W/V PEG 8K |