3KH0
Crystal structure of the Ras-association (RA) domain of RALGDS
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | CLSI BEAMLINE 08ID-1 |
Synchrotron site | CLSI |
Beamline | 08ID-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-09-11 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 0.97920 |
Spacegroup name | P 61 |
Unit cell lengths | 104.590, 104.590, 39.819 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 31.680 - 2.100 |
R-factor | 0.205 |
Rwork | 0.204 |
R-free | 0.22600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1lxd |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | BUSTER (2.8.0) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 40.000 | 40.000 | 2.180 |
High resolution limit [Å] | 2.100 | 4.520 | 2.100 |
Rmerge | 0.161 | 0.089 | 0.658 |
Number of reflections | 14288 | ||
<I/σ(I)> | 5.8 | ||
Completeness [%] | 96.7 | 99.8 | 82.5 |
Redundancy | 6.7 | 10.8 | 2.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 291 | 2.0M ammonium sulfate, 2.0% PEG400, 0.1m sodium HEPES. 1:100 (w/w) endoproteinase Glu-C were present in the crystallization drop, pH 7.5, vapor diffusion, sitting drop, temperature 291K, VAPOR DIFFUSION, SITTING DROP |