3P2L
Crystal Structure of ATP-dependent Clp protease subunit P from Francisella tularensis
Experimental procedure
Experimental method | SAD |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-07-13 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.97921 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 120.523, 128.823, 98.030 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 40.450 - 2.295 |
R-factor | 0.188 |
Rwork | 0.186 |
R-free | 0.22600 |
Structure solution method | SAD |
RMSD bond length | 0.011 |
RMSD bond angle | 1.294 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | HKL-3000 |
Refinement software | PHENIX ((phenix.refine: 1.6.4_486)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.340 |
High resolution limit [Å] | 2.300 | 2.300 |
Number of reflections | 68634 | |
<I/σ(I)> | 9.2 | 2.6 |
Completeness [%] | 99.9 | 99.9 |
Redundancy | 8.4 | 8.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 289 | 0.2 M sodium chloride, 0.1 M sodium/potassium phosphate pH 6.5, 50 % (v/v) PEG200, VAPOR DIFFUSION, SITTING DROP, temperature 289K |