2P88
Crystal structure of N-succinyl Arg/Lys racemase from Bacillus cereus ATCC 14579
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X4A |
Synchrotron site | NSLS |
Beamline | X4A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-09-15 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.97915 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 135.953, 94.610, 135.956 |
Unit cell angles | 90.00, 90.16, 90.00 |
Refinement procedure
Resolution | 24.420 - 2.400 |
R-factor | 0.221 |
Rwork | 0.221 |
R-free | 0.23900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1tkk |
RMSD bond length | 0.008 |
RMSD bond angle | 1.300 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 25.000 |
High resolution limit [Å] | 2.400 |
Rmerge | 0.076 |
Number of reflections | 123039 |
Completeness [%] | 91.2 |
Redundancy | 6.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 293 | 10% PEG MME 5000, 0.1 M Hepes, 5% Tacsimate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K |