6YXA
Structure of the bifunctional Rel enzyme from B. subtilis
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID29 |
Synchrotron site | ESRF |
Beamline | ID29 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2017-02-15 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 0.979 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 130.152, 130.152, 157.621 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 48.720 - 3.950 |
R-factor | 0.2655 |
Rwork | 0.264 |
R-free | 0.28390 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1vj7 chain B |
RMSD bond length | 0.003 |
RMSD bond angle | 0.552 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | PHENIX (1.18_3845) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 48.720 | 4.090 |
High resolution limit [Å] | 3.950 | 3.950 |
Rpim | 0.043 | 0.528 |
Number of reflections | 12337 | 1158 |
<I/σ(I)> | 10.04 | |
Completeness [%] | 99.3 | |
Redundancy | 14.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293 | 1 M Lithium chloride, 0.1 M Bicine pH 9.0, 10% PEG6000 (w/v), final pH 9.0 |