5E2G
Crystal Structure of D-alanine Carboxypeptidase AmpC from Burkholderia cenocepacia
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2015-03-20 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.97927 |
Spacegroup name | P 32 |
Unit cell lengths | 85.965, 85.965, 90.399 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 34.420 - 1.651 |
R-factor | 0.1528 |
Rwork | 0.150 |
R-free | 0.18920 |
Structure solution method | SAD |
RMSD bond length | 0.006 |
RMSD bond angle | 0.885 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | HKL-3000 |
Refinement software | PHENIX ((1.10pre_2104: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.680 |
High resolution limit [Å] | 1.650 | 1.650 |
Rmerge | 0.778 | |
Number of reflections | 87979 | |
<I/σ(I)> | 20.97 | 1.24 |
Completeness [%] | 97.9 | 80.2 |
Redundancy | 4 | 2.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 4.6 | 289 | 0.5 M potassium thioccyanate, 0.1 M sodium acetate pH 4.6 |