6A0A
Structure of a triple-helix region of human collagen type III
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL18U1 |
| Synchrotron site | SSRF |
| Beamline | BL18U1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2018-05-27 |
| Detector | DECTRIS PILATUS3 S 6M |
| Wavelength(s) | 0.979304897 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 31.335, 22.607, 41.259 |
| Unit cell angles | 90.00, 90.21, 90.00 |
Refinement procedure
| Resolution | 18.334 - 1.502 |
| R-factor | 0.1715 |
| Rwork | 0.170 |
| R-free | 0.19970 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2wuh |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.539 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.11.1_2575: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.530 |
| High resolution limit [Å] | 1.500 | 1.500 |
| Rmerge | 0.070 | 0.118 |
| Number of reflections | 8324 | 447 |
| <I/σ(I)> | 17.26 | |
| Completeness [%] | 87.9 | |
| Redundancy | 3.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 289 | 0.2M Na Chloride, 0.1M Bis-Tris pH 6.5, 25% w/v PEG 3350 |
