1WZE
Structural basis for alteration of cofactor specificity of Malate dehydrogenase from Thermus flavus
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PHOTON FACTORY BEAMLINE AR-NW12A |
Synchrotron site | Photon Factory |
Beamline | AR-NW12A |
Temperature [K] | 95 |
Detector technology | CCD |
Collection date | 2003-06-03 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 1.0000 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 70.400, 84.940, 116.940 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 48.160 - 2.000 |
R-factor | 0.193 |
Rwork | 0.193 |
R-free | 0.22800 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1bmd |
RMSD bond length | 0.005 |
RMSD bond angle | 1.200 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | CCP4 |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 48.160 | 2.130 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.049 | |
Number of reflections | 43099 | |
Completeness [%] | 90.1 | 84.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 293 | PEG 4000, dithiothreitol, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |