1KSF
Crystal Structure of ClpA, an HSP100 chaperone and regulator of ClpAP protease: Structural basis of differences in Function of the Two AAA+ ATPase domains
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X9B |
Synchrotron site | NSLS |
Beamline | X9B |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 1.000 |
Spacegroup name | P 65 |
Unit cell lengths | 124.107, 124.107, 97.042 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 20.000 - 2.600 |
R-factor | 0.22075 |
Rwork | 0.216 |
R-free | 0.30400 * |
RMSD bond length | 0.016 * |
RMSD bond angle | 1.980 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CCP4 |
Refinement software | REFMAC (5.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | |
High resolution limit [Å] | 2.600 | 2.600 |
Rmerge | 0.493 | |
Number of reflections | 22312 | |
Completeness [%] | 100.0 | 100 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 21 * | iso-propanol, pH 7.5, VAPOR DIFFUSION, HANGING DROP at 294K |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 21 * | iso-propanol, pH 7.5, VAPOR DIFFUSION, HANGING DROP at 294K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | ammonium sulfate | 50 (%sat) | |
10 | 1 | reservoir | isopropanol | 8 (%) | |
11 | 1 | reservoir | sodium azide | 0.01 (%) | |
2 | 1 | drop | protein | 12 (mg/ml) | |
3 | 1 | drop | HEPES | 0.1 (M) | pH7.5 |
4 | 1 | drop | glycerol | 10 (%) | |
5 | 1 | drop | ATPgammaS | 8 (mM) | or ADP |
6 | 1 | drop | 40 (mM) | ||
7 | 1 | reservoir | HEPES | 0.1 (M) | pH7.5 |
8 | 1 | reservoir | 0.5 (M) | ||
9 | 1 | reservoir | glycerol | 5 (%) |