4A0Q
Activated Conformation of Integrin alpha1 I-Domain mutant
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-1 |
Synchrotron site | ESRF |
Beamline | ID14-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-02-27 |
Detector | ADSC QUANTUM 210 |
Spacegroup name | P 3 |
Unit cell lengths | 95.470, 95.470, 37.719 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 20.000 - 1.900 |
R-factor | 0.18583 |
Rwork | 0.184 |
R-free | 0.22884 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1pt6 |
RMSD bond length | 0.014 |
RMSD bond angle | 1.461 |
Data reduction software | XDS |
Data scaling software | SCALEPACK |
Phasing software | MOLREP |
Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 47.740 | 2.050 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.090 | 0.420 |
Number of reflections | 30076 | |
<I/σ(I)> | 20.1 | 4.1 |
Completeness [%] | 99.3 | 99.2 |
Redundancy | 5.7 | 5.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | PROTEIN WAS CRYSTALLIZED FROM 1.6 M TRI-SODIUM CITRATE. |