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 |