3Q7H
Structure of the ClpP subunit of the ATP-dependent Clp Protease from Coxiella burnetii
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-D |
Synchrotron site | APS |
Beamline | 21-ID-D |
Temperature [K] | 110 |
Detector technology | CCD |
Collection date | 2009-12-10 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 0.97920 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 101.912, 137.469, 127.784 |
Unit cell angles | 90.00, 109.03, 90.00 |
Refinement procedure
Resolution | 37.490 - 2.500 |
R-factor | 0.172 |
Rwork | 0.170 |
R-free | 0.20770 |
Structure solution method | SAD |
RMSD bond length | 0.009 |
RMSD bond angle | 1.119 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | SHELXS |
Refinement software | PHENIX (1.6.4_486) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 37.500 | 2.590 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.103 | 0.563 |
Number of reflections | 115464 | |
<I/σ(I)> | 17.3 | 3.4 |
Completeness [%] | 99.9 | 99.9 |
Redundancy | 6.8 | 6.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 298 | 10% PEG400, 10mM calcium chloride, 100mM potassium chloride, 50mM HEPES, pH 7, VAPOR DIFFUSION, HANGING DROP, temperature 298K |