9C1A
Crystal structure of GDP-bound human M-RAS protein in crystal form I
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 17-ID |
Synchrotron site | APS |
Beamline | 17-ID |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2021-11-14 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 1.0 |
Spacegroup name | P 6 2 2 |
Unit cell lengths | 108.653, 108.653, 65.759 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 54.330 - 1.960 |
R-factor | 0.1747 |
Rwork | 0.172 |
R-free | 0.19990 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.004 |
RMSD bond angle | 0.876 |
Data reduction software | autoPROC |
Data scaling software | autoPROC |
Phasing software | PHASER |
Refinement software | PHENIX (1.19.1_4122) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 54.330 | 2.030 |
High resolution limit [Å] | 1.960 | 1.960 |
Rmeas | 0.202 | 1.732 |
Rpim | 0.032 | 0.293 |
Number of reflections | 16016 | 1643 |
<I/σ(I)> | 19.82 | 2.5 |
Completeness [%] | 94.0 | 99.88 |
Redundancy | 38.3 | |
CC(1/2) | 1.000 | 0.943 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 295 | 0.2M CaCl2, 20% PEG3350 |