5DT9
Crystal structure of a putative D-Erythronate-4-Phosphate Dehydrogenase from Vibrio cholerae
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU MICROMAX-007 HF |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2015-07-31 |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 1.5418 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 145.775, 145.775, 62.031 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 25.000 - 2.663 |
R-factor | 0.1953 |
Rwork | 0.193 |
R-free | 0.24030 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3oet |
RMSD bond length | 0.003 |
RMSD bond angle | 1.385 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | PHENIX (phenix.phaser) |
Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.000 | 2.710 |
High resolution limit [Å] | 2.660 | 2.660 |
Rmerge | 0.092 | 0.462 |
Number of reflections | 18676 | |
<I/σ(I)> | 14.39 | |
Completeness [%] | 94.8 | 94.9 |
Redundancy | 4.9 | 4.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 293 | 2 M ammonium sulfate, 0.1M Hepes pH 7.5, 2% PEG400, 1 mM Glutamic acid |