3EE0
Crystal Structure of the W215A/E217A Mutant of Human Thrombin (space group P2(1)2(1)2(1))
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 | 2008-02-29 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.9 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 40.142, 60.007, 120.011 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 26.840 - 2.750 |
| R-factor | 0.239 |
| Rwork | 0.239 |
| R-free | 0.32300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1tq0 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.300 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP (from ccp4) |
| Refinement software | CNS (1.2) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 2.800 |
| High resolution limit [Å] | 2.700 | 2.700 |
| Rmerge | 0.089 | 0.332 |
| Number of reflections | 8182 | |
| <I/σ(I)> | 14.7 | 2.5 |
| Completeness [%] | 96.3 | 78.3 |
| Redundancy | 5.4 | 2.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 295 | 0.1M MES, 30% PEG 400, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K |
