3BEF
Crystal structure of thrombin bound to the extracellular fragment of PAR1
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 14-BM-C |
Synchrotron site | APS |
Beamline | 14-BM-C |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-12-03 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.9 |
Spacegroup name | P 1 |
Unit cell lengths | 46.060, 50.342, 85.078 |
Unit cell angles | 76.89, 84.30, 73.69 |
Refinement procedure
Resolution | 28.000 - 2.200 |
R-factor | 0.207 |
Rwork | 0.207 |
R-free | 0.24800 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1shh |
RMSD bond length | 0.006 |
RMSD bond angle | 1.300 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | MOLREP (from ccp4) |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 | 2.280 |
High resolution limit [Å] | 2.200 | 2.200 |
Rmerge | 0.061 | 0.221 |
Number of reflections | 34055 | |
<I/σ(I)> | 12.3 | 3.1 |
Completeness [%] | 94.0 | 87.7 |
Redundancy | 2.4 | 2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 285 | 100mM MES, 30% PEG 4000, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 285K |