3FK2
Crystal structure of the RhoGAP domain of human glucocorticoid receptor DNA-binding factor 1
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 | 2008-11-28 |
| Detector | ADSC Q315 |
| Wavelength(s) | 0.97883 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 165.025, 72.408, 72.863 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 36.431 - 2.800 |
| R-factor | 0.226 |
| Rwork | 0.223 |
| R-free | 0.27300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2osa |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.005 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | PHENIX |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 40.000 | 40.000 | 2.900 |
| High resolution limit [Å] | 2.800 | 6.030 | 2.800 |
| Rmerge | 0.157 | 0.057 | 0.598 |
| Number of reflections | 21961 | ||
| <I/σ(I)> | 5 | ||
| Completeness [%] | 98.1 | 99 | 89 |
| Redundancy | 5.1 | 5.4 | 3.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6 | 291 | 26% PEG 3350, 0.1M Bis-Tris, 0.2M lithium sulfate, 0.001M DTT, 1:100 (w/w) trypsin, pH 6.0, vapor diffusion, sitting drop, temperature 291K |






