8YV3
The heterotrimer structure of peptides derived from human collagen type I
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU FR-X |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2024-01-30 |
| Detector | RIGAKU |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 1 |
| Unit cell lengths | 30.490, 33.043, 38.519 |
| Unit cell angles | 82.17, 77.73, 69.64 |
Refinement procedure
| Resolution | 30.910 - 1.680 |
| R-factor | 0.1954 |
| Rwork | 0.194 |
| R-free | 0.23320 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.756 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | BALBES |
| Refinement software | PHENIX ((1.20.1_4487: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.910 | 1.740 |
| High resolution limit [Å] | 1.680 | 1.680 |
| Number of reflections | 11231 | 220 |
| <I/σ(I)> | 19.86 | |
| Completeness [%] | 71.7 | |
| Redundancy | 3.8 | |
| CC(1/2) | 0.998 | 0.810 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 289 | 0.2 M Ammonium Sulfate. 0.1 M Tris:HCI pH 8.5 25%(w/v) PEG 3350 |
