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 |