8J2C
Structure of the C-terminal subenzyme of the malonyl-CoA reductase from Chloroflexus aurantiacus, mutant N940V/K1106W/S1114R
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRF BEAMLINE BL19U1 |
Synchrotron site | SSRF |
Beamline | BL19U1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2017-06-23 |
Detector | DECTRIS PILATUS3 6M |
Wavelength(s) | 0.97774 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 89.273, 133.029, 74.119 |
Unit cell angles | 90.00, 100.50, 90.00 |
Refinement procedure
Resolution | 73.265 - 1.700 |
R-factor | 0.17 |
Rwork | 0.169 |
R-free | 0.18800 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.010 |
RMSD bond angle | 0.930 |
Data reduction software | XDS (version (Nov 1, 2016, built on 20170215) |
Data scaling software | Aimless (0.5.29) |
Phasing software | PHASER (2.7.17) |
Refinement software | BUSTER (2.10.2) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 73.265 | 1.702 |
High resolution limit [Å] | 1.697 | 1.697 |
Rmeas | 0.063 | 0.674 |
Rpim | 0.024 | 0.277 |
Number of reflections | 91959 | 734 |
<I/σ(I)> | 17.3 | 2.2 |
Completeness [%] | 98.2 | 76.1 |
Redundancy | 6.7 | 5.7 |
CC(1/2) | 0.999 | 0.815 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293 | The protein was crystallized in drops containing 1.5 ul protein solution (5 mg/ml) and 1.5 ul reservoir solution (1.1 M ammonium tartrate pH 7.0) |