3S02
The crystal structure of the periplasmic domain of Helicobacter pylori MotB (residues 103-256)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-4 |
Synchrotron site | ESRF |
Beamline | ID14-4 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2007-11-04 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 1.004 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 75.803, 75.803, 140.811 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 65.650 - 2.500 |
R-factor | 0.184 |
Rwork | 0.181 |
R-free | 0.24080 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.015 |
RMSD bond angle | 1.505 |
Data reduction software | MOSFLM |
Data scaling software | SCALA (3.3.1) |
Phasing software | PHASER |
Refinement software | REFMAC (5.5.0072) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 65.650 | |
High resolution limit [Å] | 2.500 | |
Rmerge | 0.090 | |
Total number of observations | 10921 | |
Number of reflections | 16761 | |
<I/σ(I)> | 14.5 | |
Completeness [%] | 99.9 | |
Redundancy | 5.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293 | 100 mM MES pH 6.5, 6% PEG 20k, VAPOR DIFFUSION, SITTING DROP, temperature 293K |