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 |
