8HHI
Crystal structure of a triple-helix region of human collagen type III
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRF BEAMLINE BL02U1 |
Synchrotron site | SSRF |
Beamline | BL02U1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2022-09-30 |
Detector | Bruker Platinum 135 |
Wavelength(s) | 0.9792 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 23.728, 94.646, 56.843 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 36.370 - 1.400 |
R-factor | 0.161 |
Rwork | 0.156 |
R-free | 0.20900 |
Structure solution method | AB INITIO PHASING |
RMSD bond length | 0.005 |
RMSD bond angle | 1.229 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | PHASER |
Refinement software | PHENIX (1.18.1_3865) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.450 |
High resolution limit [Å] | 1.400 | 1.400 |
Rmerge | 0.039 | 0.265 |
Rpim | 0.013 | 0.153 |
Number of reflections | 23874 | 2412 |
<I/σ(I)> | 27.25 | 4.04 |
Completeness [%] | 91.2 | 94.67 |
Redundancy | 8.2 | 3.8 |
CC(1/2) | 0.990 | 0.941 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 293 | Ammonium sulfate, 0.1 M BIS-TRIS pH 5.4, 26 % PEG 2000 |