2F6I
Crystal structure of the ClpP protease catalytic domain from Plasmodium falciparum
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X25 |
| Synchrotron site | NSLS |
| Beamline | X25 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-09-17 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.1 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 158.300, 196.460, 139.170 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 2.450 |
| R-factor | 0.211 |
| Rwork | 0.210 |
| R-free | 0.23800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1tyf |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.000 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.540 |
| High resolution limit [Å] | 2.450 | 2.450 |
| Number of reflections | 78895 | |
| Completeness [%] | 99.2 | 98.5 |
| Redundancy | 7.5 | 4.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 298 | PEG MME 550, Ammonium sulfate, cacodylate buffer., pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
