2VVR
Crystal structure of the H99N mutant of ribose-5-phosphate isomerase B from E. coli soaked with ribose 5-phosphate
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 110 |
| Detector technology | CCD |
| Collection date | 2007-03-05 |
| Detector | ADSC CCD |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 89.701, 51.862, 207.209 |
| Unit cell angles | 90.00, 115.55, 90.00 |
Refinement procedure
| Resolution | 40.000 - 2.100 |
| R-factor | 0.19 |
| Rwork | 0.188 |
| R-free | 0.23700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1nn4 |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.175 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.490 | 2.210 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Rmerge | 0.110 | 0.170 |
| Number of reflections | 50635 | |
| <I/σ(I)> | 14.1 | 5.8 |
| Completeness [%] | 99.9 | 99.9 |
| Redundancy | 3.6 | 3.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 20% PEG 3350, 0.1 M MES PH6 |
