Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL45XU |
| Synchrotron site | SPring-8 |
| Beamline | BL45XU |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2021-07-04 |
| Detector | DECTRIS PILATUS3 6M |
| Wavelength(s) | 1 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 103.575, 42.537, 95.283 |
| Unit cell angles | 90.00, 110.58, 90.00 |
Refinement procedure
| Resolution | 48.530 - 1.960 |
| R-factor | 0.19181 |
| Rwork | 0.189 |
| R-free | 0.24906 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.585 |
| Data reduction software | XDS (CCP4) |
| Data scaling software | Aimless |
| Refinement software | REFMAC (5.8.0258) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 48.530 | 2.010 |
| High resolution limit [Å] | 1.960 | 1.960 |
| Rmerge | 0.119 | 0.660 |
| Number of reflections | 28236 | 1980 |
| <I/σ(I)> | 7.8 | 2.1 |
| Completeness [%] | 99.9 | 99.5 |
| Redundancy | 5.2 | 5.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293.15 | KRAS(G/C)-RNK07311-HSP90a complex was crystallized by sitting drop with vapor diffusion against 0.05M CaCl2, 0.1M Bis-Tris pH6.5, 30% PEGMME550 (drop size: 200 nl protein + 180nl reservoir + 20nl lysozyme seed). |
