2VDF
Structure of the OpcA adhesion from Neisseria meningitidis determined by crystallization from the cubic mesophase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | CHESS BEAMLINE F1 |
Synchrotron site | CHESS |
Beamline | F1 |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | ADSC CCD |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 37.860, 42.500, 150.300 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 10.000 - 1.950 |
R-factor | 0.227 |
Rwork | 0.224 |
R-free | 0.27200 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1k24 |
RMSD bond length | 0.007 |
RMSD bond angle | 1.150 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.060 |
High resolution limit [Å] | 1.950 | 1.950 |
Rmerge | 0.099 | 0.490 |
Number of reflections | 18131 | |
<I/σ(I)> | 13.1 | 2.7 |
Completeness [%] | 98.8 | 99.8 |
Redundancy | 4.8 | 4.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | LIPIDIC CUBIC PHASE | 293 | 18%(V/V) PEG400, 0.1 M POTASSIUM SULFATE, 0.05 M HEPES, PH 7.0 |