3EO2
Crystal structure of the RhoGEF domain of human neuroepithelial cell-transforming gene 1 protein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-D |
| Synchrotron site | APS |
| Beamline | 23-ID-D |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-08-11 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.97945 |
| Spacegroup name | P 64 |
| Unit cell lengths | 95.629, 95.629, 62.887 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 30.000 - 2.600 |
| R-factor | 0.215 |
| Rwork | 0.213 |
| R-free | 0.25000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2z0q |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.123 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0044) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.690 |
| High resolution limit [Å] | 2.600 | 5.600 | 2.600 |
| Rmerge | 0.095 | 0.047 | 0.526 |
| Number of reflections | 9673 | ||
| <I/σ(I)> | 12.9 | ||
| Completeness [%] | 95.1 | 98.4 | 65.3 |
| Redundancy | 8.8 | 9.6 | 2.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.8 | 1.0M sodium citrate, 0.1M sodium cacodylate, 5% ethylene glycol, crystallized in the presence of 1:100 (w/w) subtilisin, pH 4.8, vapor diffusion, hanging drop |
