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 |