5OU7
Crystal structure of the Glycoprotein VI loop truncation mutant PAVS-PAPYKN
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SLS BEAMLINE X06SA |
Synchrotron site | SLS |
Beamline | X06SA |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2013-08-22 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 0.99999 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 78.650, 44.050, 117.660 |
Unit cell angles | 90.00, 104.69, 90.00 |
Refinement procedure
Resolution | 113.810 - 1.900 |
R-factor | 0.22309 |
Rwork | 0.221 |
R-free | 0.25967 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2gi7 |
RMSD bond length | 0.011 |
RMSD bond angle | 1.480 |
Data reduction software | iMOSFLM (1.0.7) |
Data scaling software | Aimless (0.1.30) |
Phasing software | PHASER (2.7.0) |
Refinement software | REFMAC (5.8.0073) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 113.810 | 1.940 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.081 | 1.080 |
Number of reflections | 58873 | 3656 |
<I/σ(I)> | 5 | 1.1 |
Completeness [%] | 95.1 | 93.3 |
Redundancy | 2.1 | 2.1 |
CC(1/2) | 0.990 | 0.620 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 4 | 293 | 0.1 M phosphate-citrate buffer pH 4.0 40% (v/v) PEG-300 |