9C1B
Crystal structure of GDP-bound human M-RAS protein in crystal form II
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 1 |
Unit cell lengths | 53.724, 55.604, 67.770 |
Unit cell angles | 103.74, 90.14, 93.64 |
Refinement procedure
Resolution | 41.940 - 2.270 |
R-factor | 0.2021 |
Rwork | 0.199 |
R-free | 0.24690 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.002 |
RMSD bond angle | 0.527 |
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] | 41.940 | 2.351 |
High resolution limit [Å] | 2.270 | 2.270 |
Rmeas | 0.087 | 0.363 |
Rpim | 0.049 | 0.207 |
Number of reflections | 32348 | 3405 |
<I/σ(I)> | 11.81 | 3.71 |
Completeness [%] | 91.3 | |
Redundancy | 2.7 | |
CC(1/2) | 0.985 | 0.708 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 295 | 20% PEG3350 |