2QMC
Crystal Structure of Helicobacter Pylori Gamma-Glutamyltranspeptidase T380A Mutant
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 | 2007-03-10 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.9 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 57.140, 106.674, 87.194 |
| Unit cell angles | 90.00, 104.96, 90.00 |
Refinement procedure
| Resolution | 33.350 - 1.550 |
| R-factor | 0.19 |
| Rwork | 0.187 |
| R-free | 0.21800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2nqo |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.354 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.610 |
| High resolution limit [Å] | 1.550 | 1.550 |
| Rmerge | 0.084 | 0.538 |
| Number of reflections | 135161 | |
| <I/σ(I)> | 21.3 | 2.59 |
| Completeness [%] | 93.2 | 89 |
| Redundancy | 6.6 | 5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 292 | 200 MM HEPES, 25% PEG MME2000, 5 MG/ML PROTEIN, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 292K |
