8SVL
Plasmodium falciparum M1 aminopeptidase bound to MMV1557817
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX1 |
| Synchrotron site | Australian Synchrotron |
| Beamline | MX1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-02-13 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.95370 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 74.899, 109.010, 118.030 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 42.658 - 1.504 |
| R-factor | 0.1567 |
| Rwork | 0.155 |
| R-free | 0.18900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.019 |
| RMSD bond angle | 1.703 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 44.070 | 1.530 |
| High resolution limit [Å] | 1.500 | 1.500 |
| Rmerge | 0.102 | 1.599 |
| Rmeas | 0.110 | 1.742 |
| Rpim | 0.042 | 0.685 |
| Total number of observations | 1055651 | 47886 |
| Number of reflections | 153480 | 7492 |
| <I/σ(I)> | 11.5 | 1.1 |
| Completeness [%] | 100.0 | |
| Redundancy | 6.9 | 6.4 |
| CC(1/2) | 0.999 | 0.431 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 298 | 22% (v/v) PEG 8000, 10% (v/v) glycerol, 0.1 M Tris pH 8.5, 0.2 M MgCl2 |
