9RIF
The histone fold domain heterodimer of oocyst rupture proteins 1 and 2 from Plasmodium berghei
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-2 |
| Synchrotron site | ESRF |
| Beamline | ID23-2 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2023-06-23 |
| Detector | DECTRIS EIGER X 9M |
| Wavelength(s) | 0.87313 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 82.665, 112.922, 145.241 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 66.700 - 3.100 |
| R-factor | 0.2747 |
| Rwork | 0.274 |
| R-free | 0.29500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.841 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | MOLREP |
| Refinement software | PHENIX ((1.21.2_5419)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 82.700 | 3.300 |
| High resolution limit [Å] | 3.100 | 3.100 |
| Rmerge | 0.175 | 1.295 |
| Rmeas | 0.189 | 1.395 |
| Number of reflections | 25331 | 4518 |
| <I/σ(I)> | 12 | 2.3 |
| Completeness [%] | 99.8 | 99.8 |
| Redundancy | 13.2 | |
| CC(1/2) | 0.997 | 0.849 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293 | 25% (w/v) PEG 3500, 0.2 M lithium sulphate (LiSO4) and 0.1 M HEPES pH 7.5 |






