2OVJ
The crystal structure of the human Rac GTPase activating protein 1 (RACGAP1) MgcRacGAP.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X10SA |
| Synchrotron site | SLS |
| Beamline | X10SA |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-12-16 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 1.00000 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 52.913, 53.548, 67.979 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 42.070 - 1.490 |
| R-factor | 0.15307 |
| Rwork | 0.152 |
| R-free | 0.17611 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1f7c |
| RMSD bond length | 0.018 |
| RMSD bond angle | 1.703 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 42.070 | 1.540 |
| High resolution limit [Å] | 1.490 | 1.490 |
| Rmerge | 0.075 | 0.491 |
| Number of reflections | 32274 | |
| Completeness [%] | 99.9 | 99.3 |
| Redundancy | 7 | 5.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 298 | 25% PEG 3350, 0.1M BIS-TRIS, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
