1WZI
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 BL-6A |
Synchrotron site | Photon Factory |
Beamline | BL-6A |
Temperature [K] | 95 |
Detector technology | CCD |
Collection date | 2003-10-24 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 1.0000 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 70.310, 85.390, 117.700 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 28.890 - 2.000 |
R-factor | 0.196 |
Rwork | 0.196 |
R-free | 0.22900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1bmd |
RMSD bond length | 0.006 |
RMSD bond angle | 1.300 |
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] | 28.890 | 2.130 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.050 | |
Number of reflections | 48624 | |
Completeness [%] | 99.7 | 100 |
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 |