3ASA
Crystal structure of apo-LL-diaminopimelate aminotransferase from Chlamydia trachomatis
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL9-2 |
Synchrotron site | SSRL |
Beamline | BL9-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-07-05 |
Detector | MARMOSAIC 325 mm CCD |
Wavelength(s) | 0.978483 |
Spacegroup name | I 41 2 2 |
Unit cell lengths | 110.246, 110.246, 205.626 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 40.000 - 2.050 |
R-factor | 0.22899 |
Rwork | 0.227 |
R-free | 0.27683 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.012 |
RMSD bond angle | 1.433 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | REFMAC (5.5.0055) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 97.130 | 2.120 |
High resolution limit [Å] | 2.050 | 2.050 |
Number of reflections | 40054 | |
<I/σ(I)> | 2 | |
Redundancy | 7 | 6.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 298 | 10% PEG6000, 2.0M NaCl, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 298.0K |