4BGV
1.8 A resolution structure of the malate dehydrogenase from Picrophilus torridus in its apo form
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 | 2010-11-27 |
| Detector | ADSC QUANTUM 315r |
| Spacegroup name | P 41 21 2 |
| Unit cell lengths | 81.167, 81.167, 395.990 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 46.473 - 1.811 |
| R-factor | 0.1483 |
| Rwork | 0.146 |
| R-free | 0.18480 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | ONE POLY-ALA MONOMER OF OUR PREVIOUS SIRAS PTMALDH MODEL |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.096 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | PHASER (2.1.4) |
| Refinement software | PHENIX |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 46.470 | 1.910 |
| High resolution limit [Å] | 1.810 | 1.810 |
| Rmerge | 0.120 | 0.670 |
| Number of reflections | 121716 | |
| <I/σ(I)> | 6.3 | 1.3 |
| Completeness [%] | 99.8 | 98.5 |
| Redundancy | 11.5 | 10.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 3.5 | 293 | 9-14 % PEG 4000, 0.1 M CITRIC ACID PH 3.5, 293 K, 12-15 DAYS |
