5OU9
Crystal structure of Glycoprotein VI in complex with collagen-peptide (GPO)3
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID23-1 |
Synchrotron site | ESRF |
Beamline | ID23-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2013-10-08 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.97242 |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 59.720, 59.720, 319.720 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 79.930 - 2.500 |
R-factor | 0.22955 |
Rwork | 0.228 |
R-free | 0.26027 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5ou7 |
RMSD bond length | 0.008 |
RMSD bond angle | 1.564 |
Data reduction software | iMOSFLM (1.0.7) |
Data scaling software | Aimless (0.1.30) |
Phasing software | PHASER (2.7.0) |
Refinement software | REFMAC (5.8.0155) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 79.930 | 2.610 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.113 | 0.971 |
Number of reflections | 21273 | 2503 |
<I/σ(I)> | 8.5 | |
Completeness [%] | 99.9 | 100 |
Redundancy | 6.4 | 6.8 |
CC(1/2) | 0.984 | 0.646 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 9 | 293 | 0.1 M MMT-buffer pH 9.0 25% (w/v) PEG1500 |