4Z22
structure of plasmepsin II from Plasmodium Falciparum complexed with inhibitor DR718A
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | MAX II BEAMLINE I911-3 |
Synchrotron site | MAX II |
Beamline | I911-3 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2014-02-19 |
Detector | ADSC QUANTUM 210r |
Wavelength(s) | 0.97 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 52.450, 174.690, 138.970 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 41.664 - 2.620 |
R-factor | 0.2082 |
Rwork | 0.206 |
R-free | 0.25340 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2bju |
RMSD bond length | 0.003 |
RMSD bond angle | 0.814 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 87.345 | 41.664 | 2.760 |
High resolution limit [Å] | 2.620 | 8.290 | 2.620 |
Rmerge | 0.027 | 0.581 | |
Rmeas | 0.104 | ||
Rpim | 0.055 | 0.018 | 0.386 |
Total number of observations | 66480 | 2212 | 8153 |
Number of reflections | 19551 | ||
<I/σ(I)> | 9.1 | 19.4 | 2 |
Completeness [%] | 99.3 | 99 | 96.3 |
Redundancy | 3.4 | 3.2 | 3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 4.6 | 294 | 0.1M CITRIC ACID, PH 4.5, 0.4M AMMONIUM ACETATE, 21% PEG 3350, PROTEIN 10 MG/ML, 10 MM INHIBITOR (in 100% DMSO) |