5DZP
Crystal structure of Mycobacterium tuberculosis L,D-transpeptidase 2 with carbapenem drug T206 in conformation B
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) | 0.97 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 61.518, 93.874, 75.318 |
| Unit cell angles | 90.00, 92.78, 90.00 |
Refinement procedure
| Resolution | 75.230 - 2.190 |
| R-factor | 0.18305 |
| Rwork | 0.180 |
| R-free | 0.24936 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3vyn |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.915 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0103) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 75.230 | 50.000 | 2.240 |
| High resolution limit [Å] | 2.190 | 5.970 | 2.190 |
| Rmerge | 0.120 | 0.057 | 0.521 |
| Rmeas | 0.130 | 0.062 | 0.569 |
| Rpim | 0.049 | 0.024 | 0.225 |
| Total number of observations | 304379 | ||
| Number of reflections | 43836 | ||
| <I/σ(I)> | 6.3 | ||
| Completeness [%] | 99.6 | 99.6 | 99 |
| Redundancy | 6.9 | 7.1 | 6.2 |
| CC(1/2) | 0.992 | 0.900 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 291 | PEG5000MME, Ammonium sulfate |
