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Szent-Gyorgyi had previously described the more viscous form of myosin produced by slow muscle extractions as 'activated' myosin, and, since Straub's protein produced the activating effect, it was dubbed actin.
Adding ATP to a mixture of both proteins (called actomyosin) causes a decrease in viscosity.
Although no high-resolution model of actin’s filamentous form currently exists, in 2008 Sawaya’s team were able to produce a more exact model of its structure based on multiple crystals of actin dimers that bind in different places.
This model has subsequently been further refined by Sawaya and Lorenz.
The hostilities of World War II meant Szent-Gyorgyi and Straub were unable to publish the work in Western scientific journals.
Actin therefore only became well known in the West in 1945, when their paper was published as a supplement to the Acta Physiologica Scandinavica.
However the in-strand contacts and nucleotide binding sites are preserved in prokaryotes and in archaea.
Christine Oriol-Audit died in the same year that actin was first crystallized but she was the researcher that in 1977 first crystallized actin in the absence of Actin Binding Proteins (ABPs).
However, the resulting crystals were too small for the available technology of the time.
Actin is a family of globular multi-functional proteins that form microfilaments.
It is found in essentially all eukaryotic cells (the only known exception being nematode sperm), where it may be present at a concentration of over 100 μM.However, there is still no high-resolution X-ray structure of F-actin.