4B1W
Structure of the Phactr1 RPEL-2 domain bound to actin
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF |
| Synchrotron site | ESRF |
| Beamline | ID23-1 |
| Temperature [K] | 100 |
| Spacegroup name | I 4 2 2 |
| Unit cell lengths | 128.220, 128.220, 135.470 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 31.726 - 1.950 |
| R-factor | 0.1808 |
| Rwork | 0.179 |
| R-free | 0.21310 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2v52 |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.095 |
| Phasing software | PHASER |
| Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 2.110 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.150 | 0.550 |
| Number of reflections | 38647 | |
| <I/σ(I)> | 4 | 1.3 |
| Completeness [%] | 98.6 | 98.6 |
| Redundancy | 6.2 | 6.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 |






