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 |