3QVI
Crystal structure of KNI-10395 bound 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 | IMAGE PLATE |
| Collection date | 2010-08-09 |
| Detector | MAR scanner 300 mm plate |
| Wavelength(s) | 1.0000 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 88.430, 90.510, 192.410 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 39.720 - 2.500 |
| R-factor | 0.17882 |
| Rwork | 0.175 |
| R-free | 0.25187 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.018 |
| RMSD bond angle | 1.930 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0104) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 2.300 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.209 | 0.190 |
| Number of reflections | 79116 | |
| <I/σ(I)> | 9.4 | 1.05 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 6 | 7.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 4.5 | 293 | 30% (v/v) PEG 200, 0.1M Sodium Chloride, 0.1M Sodium acetate, pH 4.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
