4F14
Structure of the SH3 domain of human nebulette in complex with a peptide of XIRP2
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE X13 |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | X13 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-02-11 |
| Detector | MAR CCD 165 mm |
| Wavelength(s) | 0.8123 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 35.640, 38.420, 43.260 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 18.491 - 1.200 |
| R-factor | 0.1454 |
| Rwork | 0.144 |
| R-free | 0.17050 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.471 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine: 1.6.4_486)) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.400 | 1.230 |
| High resolution limit [Å] | 1.200 | 1.390 | 1.200 |
| Rmerge | 0.042 | ||
| Number of reflections | 18936 | ||
| <I/σ(I)> | 18.99 | ||
| Completeness [%] | 98.7 | 99 | 98 |
| Redundancy | 3.34 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8 | 293 | 10 mM ZnCl2, 20% PEG6000, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
