3OTW
Structural and Functional Studies of Helicobacter pylori Wild-Type and Mutated Proteins Phosphopantetheine adenylyltransferase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSRRC BEAMLINE BL13B1 |
| Synchrotron site | NSRRC |
| Beamline | BL13B1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-08-20 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 77.419, 119.846, 124.573 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 25.000 - 1.800 |
| R-factor | 0.18807 |
| Rwork | 0.186 |
| R-free | 0.22198 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1h1t |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.795 |
| Data reduction software | DENZO |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 26.030 | 1.850 |
| High resolution limit [Å] | 1.796 | 1.790 |
| Number of reflections | 101966 | |
| Completeness [%] | 95.0 | 99.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION | 7 | 293 | 2M (NH4)2SO4,0.2M Li2SO4, 0.1M Tris, pH 7, EVAPORATION, temperature 293K |
