4BIN
Crystal structure of the E. coli N-acetylmuramoyl-L-alanine amidase AmiC
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM30A |
Synchrotron site | ESRF |
Beamline | BM30A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2011-10-01 |
Detector | ADSC QUANTUM 315r |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 59.032, 68.442, 90.576 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 90.580 - 2.490 |
R-factor | 0.17834 |
Rwork | 0.176 |
R-free | 0.23101 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3ne8 |
RMSD bond length | 0.016 |
RMSD bond angle | 1.625 |
Data reduction software | XDS |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 49.500 | 2.560 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.200 | 1.000 |
Number of reflections | 13314 | |
<I/σ(I)> | 12.8 | 2.2 |
Completeness [%] | 99.9 | 99.8 |
Redundancy | 12.7 | 7.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 12 | 20% PEG 8000, 0.1 M CABS PH 12, 20 MM COCL2 |