6WYN
Transition metal inhibition and structural refinement of the M. tuberculosis esterase, Rv0045c
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 | 2018-07-18 |
Detector | DECTRIS PILATUS3 S 6M |
Wavelength(s) | 1.279 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 130.810, 130.810, 48.870 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 113.280 - 1.810 |
R-factor | 0.2083 |
Rwork | 0.207 |
R-free | 0.23290 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3p2m |
RMSD bond length | 0.013 |
RMSD bond angle | 1.890 |
Data reduction software | XDS |
Data scaling software | STARANISO |
Phasing software | PHASER (2.8.3) |
Refinement software | REFMAC (5.8.0258) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 113.280 | 113.280 | 1.820 |
High resolution limit [Å] | 1.720 | 5.450 | 1.720 |
Rmerge | 0.189 | 0.074 | 4.444 |
Rmeas | 0.195 | 0.076 | 5.138 |
Rpim | 0.045 | 0.017 | 2.492 |
Total number of observations | 723975 | 36712 | 8061 |
Number of reflections | 42576 | 1709 | 2124 |
<I/σ(I)> | 11.2 | 37.2 | 0.3 |
Completeness [%] | 83.5 | 100 | 29 |
Redundancy | 17 | 21.5 | 3.8 |
CC(1/2) | 0.997 | 0.999 | 0.028 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.4 | 294 | 0.2 M MgCl2, 0.1 M Imidazole pH 7.4, 18% PEG 4000, 0.01 M spermidine, 1x10^-7 M ZnCl2 |