3O9P
The structure of the Escherichia coli murein tripeptide binding protein MppA
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-4 |
| Synchrotron site | ESRF |
| Beamline | ID14-4 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-05-11 |
| Detector | ADSC QUANTUM 315r |
| Spacegroup name | P 6 |
| Unit cell lengths | 165.074, 165.074, 38.167 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 41.270 - 2.070 |
| R-factor | 0.17429 |
| Rwork | 0.172 |
| R-free | 0.21813 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2z23 |
| RMSD bond length | 0.024 |
| RMSD bond angle | 1.896 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0088) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.100 |
| High resolution limit [Å] | 2.060 | 2.060 |
| Rmerge | 0.107 | 0.553 |
| Number of reflections | 34597 | |
| <I/σ(I)> | 20.6 | 1.6 |
| Completeness [%] | 92.0 | 33.5 |
| Redundancy | 9.7 | 4.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6.5 | 293 | 20% PEG3350, 50mM zinc acetate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
