2FN4
The crystal structure of human Ras-related protein, RRAS, in the GDP-bound state
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 | 2005-12-09 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 1.00008 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 43.152, 43.152, 155.499 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 37.400 - 1.650 |
R-factor | 0.2165 |
Rwork | 0.215 |
R-free | 0.25060 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2ERY.pdb |
RMSD bond length | 0.012 |
RMSD bond angle | 1.390 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.710 |
High resolution limit [Å] | 1.650 | 1.650 |
Number of reflections | 20362 | |
Completeness [%] | 95.7 | 100 |
Redundancy | 6.1 | 5.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 293 | 1.6M Na/KPO4, 0.1M HEPES, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |