3S5H
Crystal structures of falcilysin, a M16 metalloprotease from the malaria parasite Plasmodium falciparum
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-1 |
| Synchrotron site | ESRF |
| Beamline | ID23-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-07-14 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9724 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 94.540, 107.160, 128.860 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 49.474 - 1.603 |
| R-factor | 0.2277 |
| Rwork | 0.227 |
| R-free | 0.25650 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2fge |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.578 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine: 1.6.4_486)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 49.600 | 1.690 |
| High resolution limit [Å] | 1.600 | 1.600 |
| Rmerge | 0.260 | 0.610 |
| Number of reflections | 310281 | |
| <I/σ(I)> | 3.9 | 1.3 |
| Completeness [%] | 99.3 | 97.5 |
| Redundancy | 6 | 5.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.2 | 298 | 11% PEG6000,10%PEG400,0.1M ADA, 20mM Mg acetate,20 mM Co acetate, pH 6.2, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
