3LZK
The crystal structure of a probably aromatic amino acid degradation proteiN from Sinorhizobium meliloti 1021
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-02-26 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.97929 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 62.773, 188.894, 67.736 |
Unit cell angles | 90.00, 115.17, 90.00 |
Refinement procedure
Resolution | 33.601 - 1.900 |
R-factor | 0.1876 |
Rwork | 0.185 |
R-free | 0.22650 |
Structure solution method | SAD |
RMSD bond length | 0.007 |
RMSD bond angle | 1.052 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | SHELXD |
Refinement software | PHENIX ((phenix.refine: 1.5_2)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 34.000 | 1.930 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.079 | 0.790 |
Number of reflections | 107627 | |
<I/σ(I)> | 32.3 | 1.68 |
Completeness [%] | 96.3 | 90.5 |
Redundancy | 4.6 | 4.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 293 | 0.2M CaCl2, 20% PEG3350, 1/70 chymotrypsin, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |