4Z8A
SH3-III of Drosophila Rim-binding protein bound to a Cacophony derived peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | BESSY BEAMLINE 14.2 |
| Synchrotron site | BESSY |
| Beamline | 14.2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2013-11-13 |
| Detector | RAYONIX MX-225 |
| Wavelength(s) | 0.91841 |
| Spacegroup name | I 2 2 2 |
| Unit cell lengths | 52.130, 54.246, 73.582 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 43.663 - 1.759 |
| R-factor | 0.1611 |
| Rwork | 0.159 |
| R-free | 0.20820 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4z88 |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.205 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.860 |
| High resolution limit [Å] | 1.750 | 1.750 |
| Rmerge | 0.117 | 0.557 |
| Number of reflections | 10690 | |
| <I/σ(I)> | 14.2 | 2.2 |
| Completeness [%] | 98.7 | 92.6 |
| Redundancy | 5.6 | 3.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 291 | 100 mM MES pH 6.5, 200mM Lithiumsulfat, 30% (v/v) PEG 400 |
