4AR1
Crystal Structure of the Peptidase Domain of Collagenase H from Clostridium histolyticum at 2.01 Angstrom resolution.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-4 |
| Synchrotron site | ESRF |
| Beamline | ID14-4 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-09-10 |
| Detector | ADSC QUANTUM 315r |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 79.050, 108.230, 51.270 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 46.330 - 2.010 |
| R-factor | 0.20272 |
| Rwork | 0.200 |
| R-free | 0.24953 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2y3u |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.988 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 46.330 | 2.120 |
| High resolution limit [Å] | 2.010 | 2.010 |
| Rmerge | 0.140 | 0.760 |
| Number of reflections | 29831 | |
| <I/σ(I)> | 7.8 | 2 |
| Completeness [%] | 99.8 | 99.6 |
| Redundancy | 5.8 | 5.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7.25 | 22.5% PEG3350 AND 0.15M SODIUM FORMATE, PH 7.25 |
