6DWE
Crystal structure of tryptophan synthase from M. tuberculosis - aminoacrylate- and BRD0059-bound form
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2016-03-10 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 0.97926 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 135.093, 159.396, 165.226 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 29.899 - 2.691 |
R-factor | 0.1564 |
Rwork | 0.155 |
R-free | 0.20240 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5tcj |
RMSD bond length | 0.002 |
RMSD bond angle | 0.751 |
Data reduction software | HKL-3000 |
Data scaling software | SCALEPACK |
Phasing software | HKL-3000 |
Refinement software | PHENIX (1.12_2829) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 30.000 | 30.000 | 2.750 |
High resolution limit [Å] | 2.691 | 7.300 | 2.691 |
Rmerge | 0.163 | 0.048 | 0.745 |
Rmeas | 0.178 | 0.052 | 0.827 |
Rpim | 0.070 | 0.021 | 0.352 |
Number of reflections | 98448 | 5265 | 4648 |
<I/σ(I)> | 4.3 | ||
Completeness [%] | 99.3 | 99.8 | 94.5 |
Redundancy | 6.3 | 6.2 | 5.1 |
CC(1/2) | 0.998 | 0.610 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 289 | 8% Tacsimate, pH 8.0, 20% PEG3350, 100 mM sodium malonate, pH 7.0 |