2NQO
Crystal Structure of Helicobacter pylori gamma-Glutamyltranspeptidase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 14-BM-C |
Synchrotron site | APS |
Beamline | 14-BM-C |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-03-04 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.90000 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 54.354, 105.206, 91.060 |
Unit cell angles | 90.00, 91.99, 90.00 |
Refinement procedure
Resolution | 28.190 - 1.900 |
Rwork | 0.197 |
R-free | 0.23900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2dbu |
RMSD bond length | 0.005 |
RMSD bond angle | 1.300 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 100.000 | 2.020 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.046 | 0.466 |
Number of reflections | 72974 | |
<I/σ(I)> | 32.3 | |
Completeness [%] | 91.5 | 77.6 |
Redundancy | 4.8 | 4.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 291 | 200 mM HEPES, 25% PEG MME2000, 5 mg/mL protein, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 291K |