2J5Q
2.15 A resolution structure of the wild type malate dehydrogenase from Haloarcula marismortui after first radiation burn (radiation damage series)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-1 |
| Synchrotron site | ESRF |
| Beamline | ID23-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-03-04 |
| Detector | ADSC CCD |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 126.976, 114.320, 124.117 |
| Unit cell angles | 90.00, 93.47, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.150 |
| R-factor | 0.2196 |
| Rwork | 0.220 |
| R-free | 0.26700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1o6z |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.491 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.270 |
| High resolution limit [Å] | 2.150 | 2.150 |
| Rmerge | 0.100 | 0.280 |
| Number of reflections | 91779 | |
| <I/σ(I)> | 11.4 | 3.4 |
| Completeness [%] | 95.5 | 89.2 |
| Redundancy | 3.3 | 3.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 3UL OF PROTEIN PLUS 4UL OF MPD WERE EQUILIBRATED AGAINST 58% MPD VIA THE SITTING DROP REVERSE VAPOUR DIFFUSION TECHNIQUE, pH 7.00 |
