2VVD
Crystal structure of the receptor binding domain of the spike protein P1 from bacteriophage PM2
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM14 |
| Synchrotron site | ESRF |
| Beamline | BM14 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-06-22 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.97912,0.90499 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 43.645, 49.055, 72.177 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 21.600 - 2.260 |
| R-factor | 0.172 |
| Rwork | 0.169 |
| R-free | 0.22800 |
| Structure solution method | MAD |
| Starting model (for MR) | NONE |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.966 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | SOLVE |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 21.600 | 2.330 |
| High resolution limit [Å] | 2.260 | 2.260 |
| Rmerge | 0.050 | 0.080 |
| Number of reflections | 6935 | |
| <I/σ(I)> | 46.5 | 27.7 |
| Completeness [%] | 90.0 | 52.5 |
| Redundancy | 12.1 | 7.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7.5 | 7.4MG/ML PROTEIN (IN 150MM NACL AND 20MM TRIS PH 7.5), 20%(W/V) PEG3350, 200MM CACL2 |
