6UR0
Crystal structure of ChoE D285N mutant acyl-enzyme
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 31-ID |
Synchrotron site | APS |
Beamline | 31-ID |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2019-08-08 |
Detector | DECTRIS PILATUS3 S 6M |
Wavelength(s) | 0.97931 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 45.649, 81.699, 81.214 |
Unit cell angles | 90.00, 99.78, 90.00 |
Refinement procedure
Resolution | 45.030 - 1.800 |
R-factor | 0.1459 |
Rwork | 0.145 |
R-free | 0.17110 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 6uqv |
RMSD bond length | 0.014 |
RMSD bond angle | 1.638 |
Data reduction software | MOSFLM |
Data scaling software | SCALA (3.3.22) |
Phasing software | MOLREP |
Refinement software | REFMAC (5.8.0222) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 80.034 | 81.699 | 1.900 |
High resolution limit [Å] | 1.800 | 5.690 | 1.800 |
Rmerge | 0.030 | 0.352 | |
Rmeas | 0.071 | 0.036 | 0.426 |
Rpim | 0.038 | 0.019 | 0.235 |
Total number of observations | 164957 | 5906 | 14704 |
Number of reflections | 48219 | 1736 | 4750 |
<I/σ(I)> | 13.7 | 30.6 | 3 |
Completeness [%] | 88.7 | 97.7 | 60.2 |
Redundancy | 3.4 | 3.4 | 3.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | MICROBATCH | 6.5 | 277 | 15% PEG20000, 0.1 M MES, pH 6.5 |