8RWL
Crystal structure of Methanopyrus kandleri malate dehydrogenase mutant 1
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE MASSIF-1 |
Synchrotron site | ESRF |
Beamline | MASSIF-1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2018-09-07 |
Detector | DECTRIS PILATUS3 2M |
Wavelength(s) | 0.966 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 78.250, 78.250, 251.300 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.920 - 2.300 |
R-factor | 0.2064 |
Rwork | 0.204 |
R-free | 0.24290 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.010 |
RMSD bond angle | 0.998 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | PHENIX (1.21_5207) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.360 |
High resolution limit [Å] | 2.300 | 2.300 |
Rmerge | 0.062 | 1.032 |
Rmeas | 0.064 | 1.113 |
Number of reflections | 35833 | 2568 |
<I/σ(I)> | 27.84 | 1.67 |
Completeness [%] | 99.9 | |
Redundancy | 18.25 | |
CC(1/2) | 1.000 | 0.578 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293.15 | 10 mM Hepes pH 7.5, 30% PEG 300 |