4HKH
Structure of the Hcp1 protein from E. coli EAEC 042 pathovar, mutants N93W-S158W
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID29 |
Synchrotron site | ESRF |
Beamline | ID29 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2012-06-28 |
Detector | ADSC QUANTUM 4r |
Wavelength(s) | 0.97625 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 84.210, 145.890, 89.850 |
Unit cell angles | 90.00, 103.42, 90.00 |
Refinement procedure
Resolution | 43.700 - 1.690 |
R-factor | 0.181 |
Rwork | 0.180 |
R-free | 0.19590 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3he1 |
RMSD bond length | 0.010 |
RMSD bond angle | 1.140 |
Data reduction software | XDS |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | BUSTER (2.11.2) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.750 |
High resolution limit [Å] | 1.690 | 1.690 |
Rmerge | 0.113 | 0.409 |
Number of reflections | 116904 | |
<I/σ(I)> | 8.1 | 2 |
Completeness [%] | 99.4 | 99.5 |
Redundancy | 3.5 | 3.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.8 | 298 | 14% PEG 3350, 50 mM bis-TRIS propane, 0.1 M Mg-formate , pH 6.8, VAPOR DIFFUSION, SITTING DROP, temperature 298K |