4OR1
Structure and mechanism of fibronectin binding and biofilm formation of enteroaggregative Escherischia coli AAF fimbriae
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | DIAMOND BEAMLINE I24 |
Synchrotron site | Diamond |
Beamline | I24 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2011-10-02 |
Detector | PSI PILATUS 6M |
Wavelength(s) | 0.9778 |
Spacegroup name | P 61 2 2 |
Unit cell lengths | 81.755, 81.755, 222.703 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 51.240 - 3.000 |
R-factor | 0.22149 |
Rwork | 0.220 |
R-free | 0.24840 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2axw |
RMSD bond length | 0.009 |
RMSD bond angle | 1.181 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | REFMAC (5.6.0062) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 51.240 | 3.160 |
High resolution limit [Å] | 3.000 | 3.000 |
Number of reflections | 9081 | |
<I/σ(I)> | 6.5 | 2.6 |
Completeness [%] | 97.0 | 98.2 |
Redundancy | 2.9 | 2.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 293 | 0.1 M BIS-TRIS, 0.2 M LiSO4, 25% PEG3350., pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |