5E51
Crystal structure of Mycobacterium tuberculosis L,D-transpeptidase 1 with Faropenem adduct
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) | 0.979 |
Spacegroup name | P 31 |
Unit cell lengths | 58.379, 58.379, 257.397 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 19.878 - 2.250 |
R-factor | 0.2586 |
Rwork | 0.258 |
R-free | 0.29600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4jmn |
RMSD bond length | 0.010 |
RMSD bond angle | 1.524 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | PHASER |
Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 19.878 | 2.330 |
High resolution limit [Å] | 2.250 | 2.250 |
Rmerge | 0.053 | 0.265 |
Number of reflections | 81604 | |
<I/σ(I)> | 20 | |
Completeness [%] | 87.8 | |
Redundancy | 6.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 291 | PEG6000, Bicine |