5EUF
The crystal structure of a protease from Helicobacter pylori
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2014-12-05 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.97918, 0.97940 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 155.159, 50.266, 147.889 |
Unit cell angles | 90.00, 94.86, 90.00 |
Refinement procedure
Resolution | 47.803 - 2.800 |
R-factor | 0.1894 |
Rwork | 0.186 |
R-free | 0.24450 |
Structure solution method | MAD |
RMSD bond length | 0.002 |
RMSD bond angle | 0.598 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | HKL-3000 |
Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 48.000 | 2.850 |
High resolution limit [Å] | 2.800 | 2.800 |
Rmerge | 0.124 | 0.701 |
Number of reflections | 27514 | |
<I/σ(I)> | 9 | 1.6 |
Completeness [%] | 95.3 | 92.1 |
Redundancy | 3.7 | 3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 289 | 0.2M Calcium Acetate, 0.1M HEPES:NaOH, 10% (w/v) PEG8000 |