The Challenge

Due to its flexible nature and strong tendency to self-associate, tropoelastin is not a good candidate for crystallographic studies. The team needed an alternative method of investigating the structure of a flexible protein in solution.

The Solution

An international team from UK, Australia, USA and Europe used beamline I22 at Diamond (along with ESRF and APS) to investigate the 3D solution structure of tropoelastin using small angle X-ray scattering. Complementary small angle X-ray (left) and neutron scattering (centre) measurements allowed identification of discrete regions of the molecule. The combined data provided details of the full length tropoelastin structure (right).

The Benefits

The small angle scattering measurements allowed the researchers to gain high quality structural information from a flexible protein. They gained an understanding of the subunit structure that governs the ability of elastin to stretch and how it attaches to cells. The team were able use this information to propose a mechanism for the self-assembly of tropoelastin to form elastin; nature’s ideal nanoscale spring.