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BSI Proteomics to Determine Structure of CF Membrane Protein

NEW YORK, March 21 (GenomeWeb News) - BSI Proteomics said last week that it will perform protein crystallization and structure determination services for the Cystic Fibrosis Foundation.


The foundation selected BSI to express, purify, crystallize, and determine the structure of the cystic fibrosis trans-conductance protein, a membrane protein that has proved difficult to purify, according to the Gaithersburg, MD.-based firm.


BSI will use its Membrane Protein Stabilization System, which has particular capabilities for stabilizing membrane, ion-channel, and other "difficult" soluble proteins, the company said. BSI claims that its technology can produce diffractable crystals in months, compared to years required for other methods.


The company did not disclose any financial terms for its agreement with the Cystic Fibrosis Foundation.

The Scan

Could Mix It Up

The US Food and Drug Administration is considering a plan that would allow for the mixing-and-matching of SARS-CoV-2 vaccines and boosters, the New York Times says.

Closest to the Dog

New Scientist reports that extinct Japanese wolf appears to be the closest known wild relative of dogs.

Offer to Come Back

The Knoxville News Sentinel reports that the University of Tennessee is offering Anming Hu, a professor who was acquitted of charges that he hid ties to China, his position back.

PNAS Papers on Myeloid Differentiation MicroRNAs, Urinary Exosomes, Maize Domestication

In PNAS this week: role of microRNAs in myeloid differentiation, exosomes in urine, and more.