5GKM
Crystal structure of the N-terminal Domain of Caseinolytic protease associated chaperone ClpD from Arabidopsis thaliana
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM14 |
Synchrotron site | ESRF |
Beamline | BM14 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2016-04-24 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 0.9537 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 38.080, 37.310, 99.980 |
Unit cell angles | 90.00, 96.08, 90.00 |
Refinement procedure
Resolution | 35.000 - 1.600 |
R-factor | 0.197 |
Rwork | 0.196 |
R-free | 0.21200 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5CTZ |
RMSD bond length | 0.018 |
RMSD bond angle | 1.706 |
Data reduction software | iMOSFLM (7.1.1) |
Data scaling software | Aimless |
Phasing software | MOLREP |
Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.630 |
High resolution limit [Å] | 1.600 | 1.600 |
Rmerge | 0.065 | 0.583 |
Number of reflections | 37033 | |
<I/σ(I)> | 9.8 | 2 |
Completeness [%] | 100.0 | 100 |
Redundancy | 4.2 | 4.1 |
CC(1/2) | 0.995 | 0.717 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6 | 291 | 20%(v/v) 2-propanol, 20%(w/v) PEG MME 2000, 100 mM MES monohydrate |