2WV1
CRYSTAL STRUCTURE OF THE HLYIIR MUTANT PROTEIN WITH RESIDUES 169-186 SUBSTITUTED BY A LINKER CONTAINING TWO THROMBIN SITES
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-4 |
| Synchrotron site | ESRF |
| Beamline | ID14-4 |
| Temperature [K] | 80 |
| Detector technology | CCD |
| Collection date | 2008-07-25 |
| Detector | ADSC CCD |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 52.315, 70.473, 139.238 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 24.730 - 2.300 |
| R-factor | 0.18951 |
| Rwork | 0.187 |
| R-free | 0.23613 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2fx0 |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.248 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0097) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 25.000 | 2.380 |
| High resolution limit [Å] | 2.300 | 2.300 |
| Rmerge | 0.080 | 0.590 |
| Number of reflections | 23639 | |
| <I/σ(I)> | 18.2 | 3.3 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 6.5 | 6.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7.5 | TRIS, SODIUM NITRATE, PEG3350, pH 7.5 |
