9TXC
N-terminal domain of ClpC from S. aureus
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE MASSIF-1 |
| Synchrotron site | ESRF |
| Beamline | MASSIF-1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2024-07-05 |
| Detector | DECTRIS EIGER X 4M |
| Wavelength(s) | 0.9677 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 60.856, 60.856, 99.294 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 38.470 - 1.780 |
| R-factor | 0.1923 |
| Rwork | 0.191 |
| R-free | 0.22050 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.701 |
| Data reduction software | XDS (20230630) |
| Data scaling software | Aimless (1.12.16) |
| Phasing software | PHASER (2.8.3) |
| Refinement software | PHENIX (1.21.2_5419) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 38.470 | 1.820 |
| High resolution limit [Å] | 1.780 | 1.780 |
| Rpim | 0.021 | 0.611 |
| Number of reflections | 18608 | 1031 |
| <I/σ(I)> | 18.2 | |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 23.4 | 24.7 |
| CC(1/2) | 0.999 | 0.617 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 291.15 | crystallization reservoirs 2.145 M (NH4)2SO4, 0.1 M MES pH 6 Protein at 7.5 mg/ml Crystallization drops contained 100 nL reservoir solution and 500 nL concentrated protein |
