5VEI
Crystal structure of the SH3 domain of human sorbin and SH3 domain-containing protein 2
Replaces: 4IGZExperimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2012-12-14 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.97911 |
| Spacegroup name | I 1 2 1 |
| Unit cell lengths | 46.202, 27.494, 58.831 |
| Unit cell angles | 90.00, 101.01, 90.00 |
Refinement procedure
| Resolution | 12.620 - 1.330 |
| R-factor | 0.186 |
| Rwork | 0.185 |
| R-free | 0.20600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3c0c |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.080 |
| Data reduction software | XDS |
| Data scaling software | Aimless (0.5.31) |
| Phasing software | PHASER |
| Refinement software | BUSTER (2.10.2) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 39.520 | 39.520 | 1.350 |
| High resolution limit [Å] | 1.330 | 7.280 | 1.330 |
| Rmerge | 0.046 | 0.016 | 1.208 |
| Rmeas | 0.055 | 0.019 | 1.423 |
| Rpim | 0.029 | 0.011 | 0.744 |
| Total number of observations | 60287 | 311 | 3042 |
| Number of reflections | 16870 | ||
| <I/σ(I)> | 14.8 | 46.7 | 1.1 |
| Completeness [%] | 99.7 | 92.7 | 99.8 |
| Redundancy | 3.6 | 3 | 3.6 |
| CC(1/2) | 0.999 | 0.999 | 0.494 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 6.5 | 291 | 28% PEG2000, 0.1 M Bis-Tris |
