3DWD
Crystal structure of the ArfGAP domain of human ARFGAP1
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 | 2008-07-09 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.97935 |
Spacegroup name | P 6 |
Unit cell lengths | 82.422, 82.422, 81.008 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 30.000 - 2.400 |
R-factor | 0.236 |
Rwork | 0.234 |
R-free | 0.27300 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2gf9 |
RMSD bond length | 0.017 |
RMSD bond angle | 1.445 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | REFMAC (5.5.0044) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 2.440 |
High resolution limit [Å] | 2.400 | 6.510 | 2.400 |
Rmerge | 0.092 | 0.037 | 0.653 |
Number of reflections | 12298 | ||
<I/σ(I)> | 8.1 | ||
Completeness [%] | 99.6 | 97.4 | 98.3 |
Redundancy | 7.4 | 7.3 | 6.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 291 | 3.5M Sodium Formate, 0.1M Tris, 1:100 chymotrypsin, pH 8.5, vapor diffusion, sitting drop, temperature 291K |