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 |
