Samantha A. Wynne

TL;DR: In this paper, the structure of the core protein of the hepatitis B virus was solved to 7.4 A resolution using electron cryomicroscopy, revealing the complete fold of the polypeptide chain, which is unlike previously solved viral capsid proteins and is largely α-helical.

TL;DR: The crystal structure of the T = 4 capsid has been solved at 3.3 A resolution, revealing a largely helical protein fold that is unusual for icosahedral viruses.

TL;DR: It is shown that SERT associates with lipid rafts in both heterologous expression systems and rat brain and that the inclusion of the transporter into lipid microdomains is critical for serotonin uptake activity, suggesting a mechanism for regulating the transporter activity and serotoninergic signaling in the central nervous system through the modulation of the cholesterol content in the cell membrane.

TL;DR: The results show significant differences in structure between the RNA- and DNA-containing cores, and it is suggested that the changes seen are related to maturation and control of envelopment, and a mechanism based on DNA synthesis for their triggering is proposed.

TL;DR: Two structures, of the apo form and of a binary complex of a previously described variant of Pyrococcus furiosus (Pfu) polymerase with an ability to fully replace dCTP with Cyanine dye-labeled d CTP in PCR and synthesise highly fluorescent “CyDNA” densely decorated with cyanine dye heterocycles are reported.