5GUI
Crystal structure of the N-terminal Domain of Caseinolytic protease associated chaperone ClpC1 from Arabidopsis thaliana
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | RRCAT INDUS-2 BEAMLINE PX-BL21 |
| Synchrotron site | RRCAT INDUS-2 |
| Beamline | PX-BL21 |
| Temperature [K] | 103 |
| Detector technology | CCD |
| Collection date | 2015-05-14 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.9794 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 40.100, 44.290, 97.560 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 17.540 - 1.200 |
| Rwork | 0.147 |
| R-free | 0.16700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3wdc |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.931 |
| Data reduction software | Aimless |
| Data scaling software | Aimless |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0107) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 17.540 | 1.260 |
| High resolution limit [Å] | 1.200 | 1.200 |
| Rmerge | 0.067 | 0.565 |
| Number of reflections | 54126 | |
| <I/σ(I)> | 9.4 | 2.5 |
| Completeness [%] | 97.9 | 98.4 |
| Redundancy | 4.8 | 4.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.6 | 293 | 0.1M SODIUM CITRATE DEHYDRATE, 1.0M AMMONIUM PHOSPHATE MONOBASIC |
