6F35
Crystal structure of the aspartate aminotranferase from Rhizobium meliloti
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM30A |
Synchrotron site | ESRF |
Beamline | BM30A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-12-16 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.97970 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 72.200, 117.280, 127.300 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 47.746 - 1.900 |
R-factor | 0.1539 |
Rwork | 0.152 |
R-free | 0.18070 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1j32 |
RMSD bond length | 0.006 |
RMSD bond angle | 0.859 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | PHASER |
Refinement software | PHENIX ((1.12_2829: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 47.750 | 1.950 |
High resolution limit [Å] | 1.900 | 1.900 |
Number of reflections | 85690 | 6128 |
<I/σ(I)> | 14.64 | 3.27 |
Completeness [%] | 99.8 | 98.1 |
Redundancy | 6.43 | 6.33 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 4.5 | 293 | 0.1 M Na acetate pH 4.5, 5% PEG 4K. The protein concentrations ranged from 5 mg/ml to 10 mg/ml. |