1V9N
Structure of Malate Dehydrogenase from Pyrococcus horikoshii OT3
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL26B1 |
Synchrotron site | SPring-8 |
Beamline | BL26B1 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2003-11-01 |
Detector | RIGAKU RAXIS |
Wavelength(s) | 0.985, 0.97914, 0.97944 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 74.190, 74.190, 127.280 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 28.680 - 2.100 |
R-factor | 0.208 |
Rwork | 0.208 |
R-free | 0.24300 |
Structure solution method | MAD |
RMSD bond length | 0.006 |
RMSD bond angle | 1.300 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | SOLVE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.230 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.073 | |
Number of reflections | 24293 | |
Completeness [%] | 99.7 | 100 |
Redundancy | 5.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | MICROBATCH | 5.1 | 295 | PEG, HEPES, LiCl2, pH 5.1, MICROBATCH, temperature 295K |