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 |
