1UWF
1.7 A resolution structure of the receptor binding domain of the FimH adhesin from uropathogenic E. coli
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-BM |
Synchrotron site | APS |
Beamline | 19-BM |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2000-12-15 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 39.906, 41.636, 97.070 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 38.270 - 1.690 |
R-factor | 0.1791 |
Rwork | 0.179 |
R-free | 0.21810 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1qun |
RMSD bond length | 0.006 |
RMSD bond angle | 1.500 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 39.000 | 1.730 |
High resolution limit [Å] | 1.690 | 1.690 |
Rmerge | 0.052 | 0.196 |
Number of reflections | 18597 | |
<I/σ(I)> | 27.25 | 8.2 |
Completeness [%] | 98.8 | 96.8 |
Redundancy | 8.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7.5 | 1.1 MM PROTEIN, 0.1 M HEPES PH 7.5, 10 % PEG6000, 5% V/V MPD |