3FNS
Crystal structure of histo-aspartic protease (HAP) from Plasmodium Falciparum
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-02-14 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.99999 |
| Spacegroup name | P 41 21 2 |
| Unit cell lengths | 89.800, 89.800, 198.700 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 2.500 |
| R-factor | 0.226 |
| Rwork | 0.225 |
| R-free | 0.27400 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2anl |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.553 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | MrBUMP |
| Refinement software | REFMAC (5.4.0057) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 2.600 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Rmerge | 0.093 | 0.822 |
| Number of reflections | 28895 | |
| <I/σ(I)> | 3.1 | |
| Completeness [%] | 99.7 | 99.6 |
| Redundancy | 9.5 | 9.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.5 | 293 | 10% PEG 3000, 0.2M Zinc acetate, 0.1M sodium acetate pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
