5F51
Structure of B. abortus WrbA-related protein A (apo)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-D |
Synchrotron site | APS |
Beamline | 21-ID-D |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2013-10-07 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 0.979 |
Spacegroup name | P 42 2 2 |
Unit cell lengths | 61.280, 61.280, 128.340 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 44.318 - 2.530 |
R-factor | 0.2405 |
Rwork | 0.239 |
R-free | 0.26800 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3b6i |
RMSD bond length | 0.003 |
RMSD bond angle | 0.715 |
Data reduction software | XDS |
Data scaling software | xia2 |
Phasing software | PHENIX (1.9_1692) |
Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 44.320 | 2.620 |
High resolution limit [Å] | 2.530 | 2.530 |
Rmerge | 0.063 | 0.698 |
Number of reflections | 8704 | |
<I/σ(I)> | 23.54 | 4.1 |
Completeness [%] | 99.7 | 99.6 |
Redundancy | 12.7 | 13.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 292 | 100 mM Sodium Acetate pH4.6, 300 mM Ammonium Sulfate, 20% PEG 2000 MME |