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 |






