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. |






