3MZF
Structure of penicillin-binding protein 5 from E. coli: 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 | 2004-03-24 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.00 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 109.780, 50.350, 84.290 |
| Unit cell angles | 90.00, 120.16, 90.00 |
Refinement procedure
| Resolution | 32.970 - 1.500 |
| R-factor | 0.189 |
| Rwork | 0.188 |
| R-free | 0.21200 |
| Structure solution method | FOURIER SYNTHESIS |
| Starting model (for MR) | 1nzo |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.225 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | CNS |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 33.000 | 1.550 |
| High resolution limit [Å] | 1.500 | 1.500 |
| Rmerge | 0.055 | 0.488 |
| Number of reflections | 61886 | |
| <I/σ(I)> | 40.1 | 1.8 |
| Completeness [%] | 96.6 | 76.3 |
| Redundancy | 6.8 | 3.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 294 | 100 MM TRIS PH 7.0, 8 % PEG 400, VAPOR DIFFUSION, SITTING DROP, temperature 294K |
