5TIK
Structural basis for inhibition of erythrocyte invasion by antibodies to Plasmodium falciparum protein CyRPA
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 | 2014-11-08 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.954 |
Spacegroup name | P 1 |
Unit cell lengths | 68.700, 83.560, 95.320 |
Unit cell angles | 96.77, 104.11, 115.21 |
Refinement procedure
Resolution | 48.262 - 3.090 |
R-factor | 0.1895 |
Rwork | 0.187 |
R-free | 0.22870 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5tih |
RMSD bond length | 0.002 |
RMSD bond angle | 0.472 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | PHENIX (1.10.1_2155) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 48.262 | 48.262 | 3.270 |
High resolution limit [Å] | 3.090 | 9.110 | 3.090 |
Rmerge | 0.120 | 0.036 | 0.739 |
Rmeas | 0.140 | 0.042 | 0.863 |
Total number of observations | 121060 | ||
Number of reflections | 32256 | 1260 | 4767 |
<I/σ(I)> | 10.84 | 28.72 | 2.11 |
Completeness [%] | 97.6 | 97.5 | 92.1 |
Redundancy | 3.753 | 3.622 | 3.664 |
CC(1/2) | 0.994 | 0.997 | 0.761 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | EVAPORATION | 298 | 9% PEG1000 9% PEG8000 0.25M potassium iodide 50 mM potassium thiocynate |