5KMQ
The structure of I379E variant of type II NADH dehydrogenase from Caldalkalibacillus thermarum
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
Synchrotron site | Australian Synchrotron |
Beamline | MX2 |
Temperature [K] | 113 |
Detector technology | CCD |
Collection date | 2015-10-18 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.954 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 72.383, 114.366, 130.462 |
Unit cell angles | 90.00, 92.04, 90.00 |
Refinement procedure
Resolution | 44.859 - 2.700 |
R-factor | 0.2252 |
Rwork | 0.223 |
R-free | 0.26920 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4nwz |
RMSD bond length | 0.006 |
RMSD bond angle | 1.052 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 47.600 | 2.770 |
High resolution limit [Å] | 2.700 | 2.700 |
Rmerge | 0.062 | 0.623 |
Number of reflections | 56903 | |
<I/σ(I)> | 11.6 | 1.6 |
Completeness [%] | 97.4 | 99.3 |
Redundancy | 3 | 3 |
CC(1/2) | 0.997 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 291 | 0.1 M Bicine/Tris buffer pH8.5 including 10% (v/v) PEG 4000, 25% (v/v) ethylene glycol and 55mM D, L-lysine |