5DHM
Crystal structure of the fimbrial protein Mfa4 from Porphyromonas gingivalis
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID23-1 |
Synchrotron site | ESRF |
Beamline | ID23-1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2014-06-16 |
Detector | PSI PILATUS 6M |
Wavelength(s) | 0.973 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 54.683, 84.536, 138.364 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 53.539 - 1.900 |
R-factor | 0.1859 |
Rwork | 0.183 |
R-free | 0.22950 |
Structure solution method | SAD |
RMSD bond length | 0.008 |
RMSD bond angle | 1.124 |
Data reduction software | XDS |
Data scaling software | SCALA |
Phasing software | SHELX |
Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 84.540 | 2.000 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.056 | 0.442 |
Number of reflections | 327588 | |
<I/σ(I)> | 16 | 3.4 |
Completeness [%] | 99.5 | 97.8 |
Redundancy | 6.4 | 6.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 291 | 5% polyglutamic acid (PGA), 20% PEG4000 and 0.1 M Tris pH 8.0. Protein was treated with a-chymotrypsin before crystallization. |