5CM9
Structural Basis for the Selectivity of Guanine Nucleotide Exchange Factors for the small G-protein Ral
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-1 |
| Synchrotron site | ESRF |
| Beamline | ID23-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2012-11-24 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.97488 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 169.877, 99.828, 111.487 |
| Unit cell angles | 90.00, 127.00, 90.00 |
Refinement procedure
| Resolution | 46.630 - 2.600 |
| R-factor | 0.27573 |
| Rwork | 0.273 |
| R-free | 0.31988 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4JGW as poly Ala model |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.925 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.700 |
| High resolution limit [Å] | 2.600 | 2.600 |
| Rmerge | 0.127 | |
| Number of reflections | 40751 | |
| <I/σ(I)> | 12.72 | 2.69 |
| Completeness [%] | 88.5 | 56.8 |
| Redundancy | 2.8 | 1.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.45 | 289 | 15% PEG 3350, 200 mM ammonium acetate, 100 mM Bis-Tris propane |
