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 |