How two cancer drugs can look the same but behave differently - revealed by serial room temperature crystallography
Many cancer cells require the enzyme glutaminase synthase C (GAC) to grow well. Consequently drugs that inhibit GAC are potential cancer treatments, and much work is being done to find the best ones. The Cerione group reports some of this work.
CHESS Director Earns Cornell Engineering Research Excellence Award
Powerful X-rays, energy tech, wireless electric-vehicle charging, big data, swarming robots, and cryo-electron microscopy are among some of the research themes that helped six faculty members earn Cornell Engineering Research Excellence Awards – the highest research honor given by the Ivy League’s top-ranked engineering college.
BioSAXS helps to explain the anti-cancer activity of green tea
EGCG, a polyphenol compound found in green tea, has a proven anti-cancer effect. Studies now suggest that EGCG works by binding to the potent anti-tumor protein p53 and stabilizing it, so that its activity against cancer is increased. Several experiments, including BioSAXS at CHESS ID7A, support this conclusion.
Wild blue wonder: X-ray beam explores food color protein
A natural food colorant called phycocyanin provides a fun, vivid blue in soft drinks, but it is unstable on grocery shelves. Cornell’s synchrotron is helping to steady it.
Progress in high-pressure crystallography at ID7B2 furthers the mission of HP-Bio
Recent developments at station ID7B2, jointly operated by MacCHESS and the HP-Bio project of CHEXS, demonstrate the use of high-pressure crystallography to examine the response of macromolecules to changes in pressure.
ACA honors staff scientist Richard Gillilan
Richard Gillilan, a MacCHESS/CHEXS staff scientist, has been named a member of the 2021 class of Fellows of the American Crystallographic Association (ACA), in recognition of his many career achievements.
Protein unfolded states populated at high and ambient pressure are similarly compact
This is perhaps the first reported study of the temperature dependence of the dimensions of the high pressure unfolded state of a protein. These measurements strongly support the notion that pressure unfolded proteins do not differ significantly from proteins which are unfolded at atmospheric pressure.
A virus recognizes the starting point on the DNA to be packaged inside its protein shell
A bacteriophage – a virus that attacks bacteria – assembles into an infectious species using a powerful nanomachine to stuff its DNA into a protein shell. In several types of phage, this genome packaging motor is composed of several copies of large and small terminase subunits (TerL and TerS, respectively) that attach to a portal into the protein procapsid.