3UPN
Structure of penicillin-binding protein A from M. tuberculosis: imipenem acyl-enzyme complex
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-11-08 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.00 |
| Spacegroup name | P 61 |
| Unit cell lengths | 122.800, 122.800, 101.100 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 37.350 - 2.200 |
| R-factor | 0.21642 |
| Rwork | 0.214 |
| R-free | 0.25822 |
| Structure solution method | FOURIER SYNTHESIS |
| Starting model (for MR) | 3lo7 |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.337 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | REFMAC |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 46.100 | 2.180 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Rmerge | 0.075 | 0.638 |
| Number of reflections | 49427 | |
| <I/σ(I)> | 37.4 | 1.7 |
| Completeness [%] | 98.1 | 89.3 |
| Redundancy | 11.3 | 7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5 | 292 | 20% PEG 3350, 0.2 M potassium nitrate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 292K |
