6ECB
Vlm2 thioesterase domain wild type structure 1
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | CLSI BEAMLINE 08ID-1 |
Synchrotron site | CLSI |
Beamline | 08ID-1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2017-08-09 |
Detector | DECTRIS PILATUS3 S 6M |
Wavelength(s) | 0.9794 |
Spacegroup name | P 4 3 2 |
Unit cell lengths | 151.399, 151.399, 151.399 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 87.410 - 1.700 |
R-factor | 0.1732 |
Rwork | 0.172 |
R-free | 0.18770 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2vsq |
RMSD bond length | 0.009 |
RMSD bond angle | 1.011 |
Data reduction software | DIALS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | PHENIX (1.13_2998) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 151.400 | 1.730 |
High resolution limit [Å] | 1.700 | 1.700 |
Rmerge | 0.063 | |
Rmeas | 0.066 | |
Rpim | 0.018 | |
Number of reflections | 64289 | 3000 |
<I/σ(I)> | 21.8 | |
Completeness [%] | 98.3 | |
Redundancy | 12.3 | |
CC(1/2) | 1.000 | 0.502 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 9.5 | 295 | 1.65 M DL-malic acid, pH 9.5, 25 mM HEPES, pH 8.0, 100 mM sodium chloride, 0.2 mM TCEP |