4F17
Crystal Structure of the alpha spectrin SH3 domain at pH 9
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM16 |
| Synchrotron site | ESRF |
| Beamline | BM16 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-03-03 |
| Detector | ADSC QUANTUM 210r |
| Wavelength(s) | 0.98 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 34.433, 42.342, 49.984 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 14.998 - 1.550 |
| R-factor | 0.2009 |
| Rwork | 0.200 |
| R-free | 0.21720 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1shg |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.917 |
| Data reduction software | DENZO |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | PHENIX (1.7.3_928) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 1.610 |
| High resolution limit [Å] | 1.550 | 1.550 |
| Rmerge | 0.056 | 0.354 |
| Number of reflections | 11117 | |
| <I/σ(I)> | 8.8 | 4.6 |
| Completeness [%] | 95.5 | 97.6 |
| Redundancy | 3.1 | 3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | capillary counterdiffusion | 9 | 298 | 0.1M Tris-HCl, 20% PEG 400, 15% PEG 4000, 10% PEG 8000, pH 9, capillary counterdiffusion, temperature 298K |
