3UXF
Structure of the fimbrial protein FimP from Actonomyces oris
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-1 |
Synchrotron site | ESRF |
Beamline | ID14-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2011-06-22 |
Detector | ADSC QUANTUM 210 |
Wavelength(s) | 0.9334 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 77.239, 176.587, 40.119 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 46.817 - 1.603 |
R-factor | 0.1708 |
Rwork | 0.170 |
R-free | 0.19610 |
Structure solution method | SAD |
RMSD bond length | 0.012 |
RMSD bond angle | 1.432 |
Data reduction software | XDS |
Data scaling software | SCALA |
Phasing software | Auto-Rickshaw |
Refinement software | PHENIX ((phenix.refine: 1.6.4_486)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 46.820 | 1.690 |
High resolution limit [Å] | 1.600 | 1.600 |
Number of reflections | 71226 | |
<I/σ(I)> | 21.4 | 5.8 |
Completeness [%] | 97.5 | 95.1 |
Redundancy | 5.4 | 2.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 291 | 20% PEG4000, 50 mM calcium chloride, 100 mM sodium acetate, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 291K |