5TIH
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 | 2016-08-19 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.954 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 79.950, 87.380, 145.140 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 38.339 - 2.440 |
R-factor | 0.1898 |
Rwork | 0.189 |
R-free | 0.21150 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5l9d |
RMSD bond length | 0.003 |
RMSD bond angle | 0.576 |
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] | 38.339 | 38.339 | 2.580 |
High resolution limit [Å] | 2.440 | 7.230 | 2.440 |
Rmerge | 0.081 | 0.035 | 0.991 |
Rmeas | 0.089 | 0.038 | 1.088 |
Total number of observations | 228722 | ||
Number of reflections | 38349 | 1571 | 5742 |
<I/σ(I)> | 14.54 | 34.5 | 2.17 |
Completeness [%] | 99.4 | 96.4 | 97.8 |
Redundancy | 5.964 | 5.391 | 5.619 |
CC(1/2) | 0.998 | 0.999 | 0.727 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | EVAPORATION | 5.5 | 298 | 11% PEG5000 monomethyl ether 0.2M NaAc |