5HUB
High-resolution structure of chorismate mutase from Corynebacterium glutamicum
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2014-10-30 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.97908 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 82.858, 24.627, 38.546 |
| Unit cell angles | 90.00, 99.43, 90.00 |
Refinement procedure
| Resolution | 40.870 - 1.060 |
| R-factor | 0.17548 |
| Rwork | 0.173 |
| R-free | 0.22021 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2vkl |
| RMSD bond length | 0.019 |
| RMSD bond angle | 2.012 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER (2.5.7) |
| Refinement software | REFMAC (5.8.0135) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.870 | 1.130 |
| High resolution limit [Å] | 1.060 | 1.060 |
| Rmerge | 0.056 | 1.937 |
| Number of reflections | 30562 | |
| <I/σ(I)> | 8.96 | 0.44 |
| Completeness [%] | 87.9 | 49.2 |
| Redundancy | 4.3 | 3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.6 | 293 | 100 mM NH4 formate, pH 6.6 100 mM KSCN 30% PEG 2000 MME |
