3PQF
Crystal structure of L-lactate dehydrogenase from Bacillus subtilis mutation H171C complexed with NAD+
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-G |
Synchrotron site | APS |
Beamline | 21-ID-G |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-02-06 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 0.98 |
Spacegroup name | P 31 |
Unit cell lengths | 133.431, 133.431, 99.088 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 30.494 - 2.490 |
R-factor | 0.1899 |
Rwork | 0.189 |
R-free | 0.23470 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.008 |
RMSD bond angle | 1.129 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | AMoRE |
Refinement software | PHENIX ((phenix.refine: 1.6_289)) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 30.494 |
High resolution limit [Å] | 2.490 |
Number of reflections | 68913 |
Completeness [%] | 100.0 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.4 | 293 | 20% PEG 4000, 0.1 M Na/K PO4, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 293K |