5E1G
Crystal structure of Mycobacterium tuberculosis L,D-transpeptidase 2 with carbapenem drug T208
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 | CCD |
| Collection date | 2015-03-16 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.978 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 61.283, 93.872, 75.358 |
| Unit cell angles | 90.00, 93.08, 90.00 |
Refinement procedure
| Resolution | 37.243 - 1.852 |
| R-factor | 0.1982 |
| Rwork | 0.197 |
| R-free | 0.22720 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3vyn |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.121 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.880 |
| High resolution limit [Å] | 1.850 | 5.020 | 1.850 |
| Rmerge | 0.069 | 0.038 | 0.458 |
| Rmeas | 0.074 | 0.041 | 0.492 |
| Rpim | 0.027 | 0.016 | 0.181 |
| Total number of observations | 517286 | ||
| Number of reflections | 71306 | ||
| <I/σ(I)> | 10.1 | ||
| Completeness [%] | 99.0 | 99.4 | 97.8 |
| Redundancy | 7.3 | 7.2 | 7.2 |
| CC(1/2) | 0.997 | 0.949 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 291 | PEG5000MME, Ammonium sulfate |
