2X5K
Structure of an active site mutant of the D-Erythrose-4-Phosphate Dehydrogenase from E. coli
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-3 |
Synchrotron site | ESRF |
Beamline | ID14-3 |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | ADSC CCD |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 134.810, 134.810, 246.110 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 55.970 - 2.370 |
R-factor | 0.16656 |
Rwork | 0.164 |
R-free | 0.20699 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2x5j |
RMSD bond length | 0.023 |
RMSD bond angle | 1.963 |
Data reduction software | XDS |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 56.000 | 2.500 |
High resolution limit [Å] | 2.370 | 2.370 |
Rmerge | 0.080 | 0.770 |
Number of reflections | 91660 | |
<I/σ(I)> | 28.1 | 4.5 |
Completeness [%] | 98.6 | 93.1 |
Redundancy | 10.2 | 5.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 24 % (W/V) PEG 1000, 100 MM TRIS-HCL BUFFER PH 8.5, 3 MM ERYTHROSE-4-PHOSPHATE |