1TR2
Crystal structure of human full-length vinculin (residues 1-1066)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 66.740, 154.080, 108.950 |
| Unit cell angles | 90.00, 90.44, 90.00 |
Refinement procedure
| Resolution | 56.860 - 2.900 |
| R-factor | 0.2356 |
| Rwork | 0.232 |
| R-free | 0.30050 |
| Structure solution method | SAD |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.945 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | SHARP |
| Refinement software | BUSTER-TNT (1.1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 56.860 | 2.980 |
| High resolution limit [Å] | 2.900 | 2.900 |
| Rmerge | 0.154 | 0.451 |
| Number of reflections | 48752 | |
| <I/σ(I)> | 21 | 1.4 |
| Completeness [%] | 100.0 | 99.7 |
| Redundancy | 23.7 | 3.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 |
