5OCG
Discovery of small molecules binding to KRAS via high affinity antibody fragment competition method.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE MASSIF-3 |
| Synchrotron site | ESRF |
| Beamline | MASSIF-3 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2015-06-22 |
| Detector | DECTRIS EIGER X 4M |
| Wavelength(s) | 0.9677 |
| Spacegroup name | H 3 |
| Unit cell lengths | 78.085, 78.085, 77.650 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 39.000 - 1.480 |
| R-factor | 0.17669 |
| Rwork | 0.175 |
| R-free | 0.20418 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4dsn |
| RMSD bond length | 0.024 |
| RMSD bond angle | 2.254 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 39.040 |
| High resolution limit [Å] | 1.450 |
| Number of reflections | 31312 |
| <I/σ(I)> | 8.2 |
| Completeness [%] | 100.0 |
| Redundancy | 5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 277 | 0.1 M TrisCl pH 8.0, 0.2 M NaOAc and 30-36 % PEG 4000 |
