The Di Cera lab recently published a paper in the May issue of the Proceedings of the National Academy of Sciences. The study is the first to show crystallization of prothrombin, a key factor in the clotting cascade. Prothrombin is the inactive form of thrombin and is converted to thrombin after the coagulation is initiated due to a vascular injury or other vascular event.
The researchers published the structure of prothrombin in a previous paper, but it was not complete and did not show how the molecule interacted with membranes and other molecules. Prothrombin contains two Kringle domains connected by a disordered linker section. Once the linker section was deleted, the researchers were able to grow prothrombin crystals at a much faster rate and revealed the full structure of the molecule.
You can read the full story in SLU Newslink.