3CON
Crystal structure of the human NRAS GTPase bound with GDP
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU FR-E |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2008-03-13 |
Detector | RIGAKU RAXIS |
Wavelength(s) | 1.5418 |
Spacegroup name | P 63 |
Unit cell lengths | 83.061, 83.061, 38.907 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 35.967 - 1.649 |
R-factor | 0.186 |
Rwork | 0.185 |
R-free | 0.21900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4q21 |
RMSD bond length | 0.016 |
RMSD bond angle | 1.530 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | REFMAC (5.3.0037) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 40.000 | 40.000 | 1.710 |
High resolution limit [Å] | 1.649 | 3.550 | 1.649 |
Rmerge | 0.065 | 0.054 | 0.469 |
Number of reflections | 18539 | ||
<I/σ(I)> | 13.9 | ||
Completeness [%] | 99.2 | 99.8 | 92.8 |
Redundancy | 9.7 | 10 | 4.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 291 | 30.0% PEG 3350, 0.2M Magnesium chloride, 0.1 M Tris-HCl, GDP was added to the concentrated protein to a final concentration of 5mM. Crystallization were set up with 1:100 chymotrypsin, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 291K |