3S0H
The crystal structure of the periplasmic domain of Helicobacter pylori MotB (residues 90-256).
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-2 |
| Synchrotron site | ESRF |
| Beamline | ID23-2 |
| Detector technology | CCD |
| Collection date | 2009-04-08 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.87 |
| Spacegroup name | P 43 |
| Unit cell lengths | 72.972, 72.972, 127.178 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 2.100 |
| R-factor | 0.1841 |
| Rwork | 0.181 |
| R-free | 0.23610 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.422 |
| Data scaling software | SCALA (3.3.1) |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0072) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 51.571 | 51.571 | 2.210 |
| High resolution limit [Å] | 2.100 | 6.640 | 2.100 |
| Rmerge | 0.098 | 0.050 | 0.343 |
| Total number of observations | 3055 | 14202 | |
| Number of reflections | 37792 | ||
| <I/σ(I)> | 6.8 | 11.4 | 2.2 |
| Completeness [%] | 97.5 | 92.3 | 98.8 |
| Redundancy | 2.6 | 2.7 | 2.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 |






