4WAT
Crystal structure of PfRh5, an essential P. falciparum ligand for invasion of human erythrocytes
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
Synchrotron site | Australian Synchrotron |
Beamline | MX2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2012-11-27 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.954 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 53.980, 86.260, 114.830 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 45.760 - 2.180 |
R-factor | 0.2041 |
Rwork | 0.202 |
R-free | 0.24730 |
RMSD bond length | 0.009 |
RMSD bond angle | 1.060 |
Refinement software | BUSTER (2.10.0) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 45.760 |
High resolution limit [Å] | 2.180 |
Number of reflections | 28700 |
<I/σ(I)> | 5.44 |
Completeness [%] | 99.9 |
Redundancy | 7.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | EVAPORATION | 281 | 8-12% PEG3350 or PEG4000, 0.2 M DL-malate-imidazole, pH 6.5-7.5 |