4AR8
Crystal structure of the peptidase domain of collagenase T from Clostridium tetani complexed with the peptidic inhibitor isoamyl- phosphonyl-Gly-Pro-Ala at 2.05 angstrom resolution.
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 | 2011-09-10 |
| Detector | DECTRIS PILATUS 6M |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 74.420, 102.080, 102.480 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 45.750 - 2.050 |
| R-factor | 0.22013 |
| Rwork | 0.218 |
| R-free | 0.26793 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2y3u |
| RMSD bond length | 0.005 |
| RMSD bond angle | 0.864 |
| 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] | 45.700 | 2.160 |
| High resolution limit [Å] | 2.050 | 2.050 |
| Rmerge | 0.110 | 0.590 |
| Number of reflections | 48639 | |
| <I/σ(I)> | 6 | 2 |
| Completeness [%] | 98.1 | 98.5 |
| Redundancy | 4 | 4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6.5 | 25% PEG 3350, 0.1 M NACL, 0.1 M MES PH 6.5 |
