4O2H
Crystal structure of BCAM1869 protein (RsaM homolog) 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 | 2012-06-04 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.97926 |
Spacegroup name | P 61 2 2 |
Unit cell lengths | 69.146, 69.146, 216.772 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 20.200 - 2.300 |
R-factor | 0.2166 |
Rwork | 0.215 |
R-free | 0.25680 |
Structure solution method | MIRAS |
RMSD bond length | 0.011 |
RMSD bond angle | 1.070 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | SHARP |
Refinement software | BUSTER (2.8.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.340 |
High resolution limit [Å] | 2.300 | 2.300 |
Rmerge | 0.059 | 0.924 |
Number of reflections | 14488 | |
<I/σ(I)> | 47 | 2.8 |
Completeness [%] | 99.8 | 100 |
Redundancy | 13.5 | 14.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 289 | 0.2 M Ca acetate, 10% PEG8K, 0.1 M HEPES:NaOH, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 289K |