4B1Y
Structure of the Phactr1 RPEL-3 bound to G-actin
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF |
Synchrotron site | ESRF |
Beamline | ID29 |
Temperature [K] | 100 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 52.580, 63.560, 62.570 |
Unit cell angles | 90.00, 108.83, 90.00 |
Refinement procedure
Resolution | 29.419 - 1.290 |
R-factor | 0.1515 |
Rwork | 0.150 |
R-free | 0.17440 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2v52 |
RMSD bond length | 0.007 |
RMSD bond angle | 1.296 |
Phasing software | PHASER |
Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 1.360 |
High resolution limit [Å] | 1.290 | 1.290 |
Rmerge | 0.050 | 0.420 |
Number of reflections | 98023 | |
<I/σ(I)> | 5.5 | 1.8 |
Completeness [%] | 99.7 | 99.7 |
Redundancy | 3.1 | 3.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 |