4BGU
1.50 A resolution structure of the malate dehydrogenase from Haloferax volcanii
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 | 2011-02-23 |
| Detector | ADSC QUANTUM 315r |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 143.760, 82.319, 112.750 |
| Unit cell angles | 90.00, 101.72, 90.00 |
Refinement procedure
| Resolution | 48.479 - 1.487 |
| R-factor | 0.1569 |
| Rwork | 0.156 |
| R-free | 0.17880 |
| Structure solution method | SIRAS |
| Starting model (for MR) | NONE |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.303 |
| Data reduction software | XDS (10-05-2010) |
| Data scaling software | SCALA (3.3.16) |
| Phasing software | SHARP |
| Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 48.340 | 1.580 |
| High resolution limit [Å] | 1.490 | 1.490 |
| Rmerge | 0.060 | 0.400 |
| Number of reflections | 205562 | |
| <I/σ(I)> | 21.6 | 4.9 |
| Completeness [%] | 100.0 | 99.9 |
| Redundancy | 7.4 | 7.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 8 | 293 | 31-36% PEG 400, 0.1 M TRIS HCL PH 8.0, 0.1 M MGCL2, 293 K, 2-4 DAYS |
