3GF9
Crystal structure of human Intersectin 2 RhoGEF domain
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-02-15 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.97937 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 106.249, 29.616, 86.150 |
| Unit cell angles | 90.00, 121.06, 90.00 |
Refinement procedure
| Resolution | 36.899 - 2.500 |
| R-factor | 0.224 |
| Rwork | 0.221 |
| R-free | 0.27700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ki1 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.137 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | PHENIX |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.590 |
| High resolution limit [Å] | 2.500 | 5.380 | 2.500 |
| Rmerge | 0.091 | 0.035 | 0.621 |
| Number of reflections | 8098 | ||
| <I/σ(I)> | 10.2 | ||
| Completeness [%] | 97.3 | 99.7 | 87.7 |
| Redundancy | 3.1 | 3.2 | 2.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 291 | 25% PEG-3350, 0.1M ammonium sulfate, 0.1M Bis-Tris, 1:100 papain protease was added, SDS-PAGE indicated that the crystallized protein had a molecular weight of 23kDa, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 291K |
