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 |