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 |






