3EAP
Crystal structure of the RhoGAP domain of ARHGAP11A
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-B |
| Synchrotron site | APS |
| Beamline | 23-ID-B |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-02-14 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.96863 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 46.066, 106.150, 107.335 |
| Unit cell angles | 90.00, 97.16, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.300 |
| R-factor | 0.23 |
| Rwork | 0.227 |
| R-free | 0.27700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1rgp |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.293 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.4.0069) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.280 |
| High resolution limit [Å] | 2.200 | 4.740 | 2.200 |
| Rmerge | 0.063 | 0.031 | 0.549 |
| Number of reflections | 49354 | ||
| Completeness [%] | 94.7 | 97.3 | 68.7 |
| Redundancy | 3.4 | 3.7 | 1.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 8 | 291 | 6% PEG 8000, 0.2M sodium chloride, 0.1M tris, pH 8.0. The protein stock solution was supplemented with 5% Ethylene Glycol, and 1:100 (m:m) Endoproteinase Glu-C. vapor diffusion, temperature 291K, VAPOR DIFFUSION |
