4B1U
Structure of the Phactr1 RPEL domain and RPEL motif directed assemblies with G-actin reveal the molecular basis for actin binding cooperativity.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF |
| Synchrotron site | ESRF |
| Beamline | ID23-1 |
| Temperature [K] | 100 |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 77.600, 77.600, 128.230 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 28.934 - 2.000 |
| R-factor | 0.1968 |
| Rwork | 0.195 |
| R-free | 0.23640 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2v52 |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.192 |
| Phasing software | PHASER |
| Refinement software | PHENIX ((PHENIX.REFINE: 1.8.1_1168)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.110 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.100 | 0.550 |
| Number of reflections | 30882 | |
| <I/σ(I)> | 5.6 | 1.3 |
| Completeness [%] | 98.9 | 98.4 |
| Redundancy | 6.6 | 6.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 |
