4ZFQ
Structure of M. tuberculosis (3,3) L,D-Transpeptidase, LdtMt5. (Meropenen-adduct form)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X6A |
| Synchrotron site | NSLS |
| Beamline | X6A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2013-12-01 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.116 |
| Spacegroup name | P 62 2 2 |
| Unit cell lengths | 99.393, 99.393, 193.384 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 29.044 - 2.799 |
| R-factor | 0.2324 |
| Rwork | 0.230 |
| R-free | 0.27660 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4z7a |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.246 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.850 |
| High resolution limit [Å] | 2.799 | 2.800 |
| Rmerge | 0.490 | |
| Number of reflections | 14630 | |
| <I/σ(I)> | 53.3 | 6.3 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 22.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.6 | 293.5 | 85 mM sodium citrate, pH 5.6, 25.5% PEG 4,000, 170 mM ammonium acetate, and 15% glycerol |
