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 |
