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 |