3S9C
Russell's viper venom serine proteinase, RVV-V in complex with the fragment (residues 1533-1546) of human factor V
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL41XU |
| Synchrotron site | SPring-8 |
| Beamline | BL41XU |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-10-13 |
| Detector | RAYONIX MX-225 |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 61 |
| Unit cell lengths | 101.200, 101.200, 44.200 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 29.210 - 1.800 |
| R-factor | 0.183 |
| Rwork | 0.183 |
| R-free | 0.21800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3s9a |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.600 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | CNS (1.3) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.860 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.047 | 0.296 |
| Number of reflections | 24029 | |
| <I/σ(I)> | 46.3 | 6.9 |
| Completeness [%] | 99.0 | 91.8 |
| Redundancy | 10.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6 | 293 | 20% PEG 3350, 0.2M zinc acetate, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
