1JMO
Crystal Structure of the Heparin Cofactor II-S195A Thrombin Complex
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SRS BEAMLINE PX14.1 |
| Synchrotron site | SRS |
| Beamline | PX14.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2001-01-30 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 1.4880 |
| Spacegroup name | P 61 |
| Unit cell lengths | 152.310, 152.310, 126.800 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 29.440 - 2.200 |
| Rwork | 0.205 |
| R-free | 0.21100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | N-terminal half of native heparin cofactor II and native S195A thrombin |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.400 * |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 29.400 * | 2.350 |
| High resolution limit [Å] | 2.200 | 2.210 |
| Rmerge | 0.080 * | 0.539 |
| Total number of observations | 475985 * | |
| Number of reflections | 77117 * | |
| <I/σ(I)> | 6.5 | 1.5 |
| Completeness [%] | 91.1 * | 62.5 |
| Redundancy | 6.2 | 2.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | unknown * | 7.4 | 298 | NH4Cl, PEG 3350, pH 7.4, VAPOR DIFFUSION, HANGING DROP at 298K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | 1 | protein | 8-10 (mg/ml) | |
| 2 | 1 | 1 | 0.06 (M) | ||
| 3 | 1 | 1 | PEG3350 | 6 (%) |
