9END
Crystal structure of Methanopyrus kandleri malate dehydrogenase mutant 3
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE MASSIF-3 |
Synchrotron site | ESRF |
Beamline | MASSIF-3 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2018-11-14 |
Detector | DECTRIS EIGER X 4M |
Wavelength(s) | 0.96770 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 78.820, 78.820, 251.510 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.780 - 1.950 |
R-factor | 0.1967 |
Rwork | 0.195 |
R-free | 0.23010 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.010 |
RMSD bond angle | 1.048 |
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 | 2.000 |
High resolution limit [Å] | 1.950 | 1.950 |
Number of reflections | 58752 | 4274 |
<I/σ(I)> | 5.93 | 1.4 |
Completeness [%] | 99.7 | 100 |
Redundancy | 7.75 | 8.18 |
CC(1/2) | 0.978 | 0.518 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 293 | 0.2 M potassium citrate tribasic monohydrate, 24% PEG 3350 |