1O6Z
1.95 A resolution structure of (R207S,R292S) mutant of malate dehydrogenase from the halophilic archaeon Haloarcula marismortui (holo form)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-2 |
Synchrotron site | ESRF |
Beamline | ID14-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2000-06-17 |
Detector | ADSC CCD |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 126.640, 114.420, 124.870 |
Unit cell angles | 90.00, 93.11, 90.00 |
Refinement procedure
Resolution | 42.260 * - 1.950 |
R-factor | 0.19365 |
Rwork | 0.190 |
R-free | 0.26300 * |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1GT2 |
RMSD bond length | 0.038 * |
RMSD bond angle | 2.450 * |
Data reduction software | XDS |
Data scaling software | BIOMOL |
Phasing software | AMoRE |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 42.260 | 2.020 |
High resolution limit [Å] | 1.950 | 1.950 |
Rmerge | 0.064 | 0.143 |
Total number of observations | 335871 * | |
Number of reflections | 100475 | 5703 * |
<I/σ(I)> | 12.86 | 4.03 |
Completeness [%] | 77.8 | 43.9 |
Redundancy | 3.34 | 2.12 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, sitting drop * | 7.6 | 4 * | 2 M NACL, 25 MM TRIS PH 7.6, 2.5 MM NADH, 50% MPD |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | HEPES | 50 (mM) | pH7.6 |
2 | 1 | drop | 4 (M) | ||
3 | 1 | drop | protein | 20 (mg/ml) | |
4 | 1 | reservoir | MPD | 62 (%(v/v)) |