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. |
