2J0P
Structure of the haem-chaperone Proteobacteria-protein HemS
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM14 |
| Synchrotron site | ESRF |
| Beamline | BM14 |
| Temperature [K] | 98 |
| Detector technology | CCD |
| Collection date | 2005-03-14 |
| Detector | MARRESEARCH |
| Spacegroup name | I 2 2 2 |
| Unit cell lengths | 74.941, 77.593, 114.291 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 1.700 |
| R-factor | 0.194 |
| Rwork | 0.192 |
| R-free | 0.22100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1u9t |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.474 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.790 |
| High resolution limit [Å] | 1.700 | 1.700 |
| Rmerge | 0.080 | 0.230 |
| Number of reflections | 36050 | |
| <I/σ(I)> | 13 | 2.4 |
| Completeness [%] | 97.5 | 98 |
| Redundancy | 11.7 | 3.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 50MM TRIS-HCL PH8.5, 1.8M AMMONIUM SULPHATE, 4% PEG400 |
