3CXN
Structure of the Urease Accessory Protein UreF from Helicobacter pylori
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 17-ID |
Synchrotron site | APS |
Beamline | 17-ID |
Detector technology | CCD |
Collection date | 2006-10-22 |
Detector | ADSC QUANTUM 210 |
Wavelength(s) | 0.97926 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 135.225, 89.418, 66.042 |
Unit cell angles | 90.00, 94.03, 90.00 |
Refinement procedure
Resolution | 26.770 - 1.550 |
R-factor | 0.188 |
Rwork | 0.187 |
R-free | 0.21100 |
Structure solution method | SAD |
RMSD bond length | 0.010 |
RMSD bond angle | 1.236 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SHARP |
Refinement software | REFMAC (refmac_5.2.0019) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 1.610 |
High resolution limit [Å] | 1.550 | 3.340 | 1.550 |
Rmerge | 0.051 | 0.036 | 0.383 |
Number of reflections | 112962 | ||
<I/σ(I)> | 13.1 | ||
Completeness [%] | 99.5 | 97.8 | 99.1 |
Redundancy | 4.2 | 4.1 | 4.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.8 | 298 | 21% PEG MME 2000, 0.1M BIS-TRIS, pH 6.8, VAPOR DIFFUSION, SITTING DROP, temperature 298.0K |