7TBB
Crystal structure of Plasmepsin X from Plasmodium falciparum
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 | PIXEL |
Collection date | 2019-11-21 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 0.9536 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 62.308, 63.152, 79.337 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 33.590 - 1.850 |
R-factor | 0.2116 |
Rwork | 0.208 |
R-free | 0.25990 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5ux4 |
RMSD bond length | 0.007 |
RMSD bond angle | 0.946 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | Auto-Rickshaw |
Refinement software | PHENIX (1.19.2_4158) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 33.590 | 1.920 |
High resolution limit [Å] | 1.850 | 1.850 |
Rpim | 0.029 | 0.041 |
Number of reflections | 27357 | 2688 |
<I/σ(I)> | 15.71 | 1.43 |
Completeness [%] | 99.9 | 99.9 |
Redundancy | 13.3 | 13.4 |
CC(1/2) | 1.000 | 0.788 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 4 | 293 | 25% (w/v) PEG1500, 10% (w/v) SPG pH 4.0 |