9RFB
Crystal Structure of Human Rac1 in Complex with the Scaffold Protein POSH (residues 321-348)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE MASSIF-1 |
| Synchrotron site | ESRF |
| Beamline | MASSIF-1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2022-07-22 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.9655 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 54.793, 54.793, 329.942 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 19.670 - 1.854 |
| Rwork | 0.195 |
| R-free | 0.22630 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.412 |
| Data reduction software | autoPROC (1.0.5 (20230222)) |
| Data scaling software | autoPROC (1.0.5 (20230222)) |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0411) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 19.670 | 2.027 |
| High resolution limit [Å] | 1.854 | 1.854 |
| Rmerge | 0.185 | 1.100 |
| Rmeas | 0.193 | 1.200 |
| Rpim | 0.052 | 0.389 |
| Number of reflections | 34144 | 1707 |
| <I/σ(I)> | 8 | 1.7 |
| Completeness [%] | 94.2 | 67 |
| Redundancy | 13.4 | |
| CC(1/2) | 0.997 | 0.812 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 277 | 0.05 M phosphate, 20% (w/v) PEG 8000. RAC1 6 mg/mL , GMPPNP 1mM, POSH 3 mM |






