This week’s #WiSEWednesday honoree needs your help! Crystallography is sometimes described as a sort of “magic” because crystals often form unpredictably, but Janet Newman is trying to figure out the science behind the “magic” by collecting and analyzing data about what conditions worked or didn’t work for various proteins – and she’s crowdsourcing some of her efforts.

 

A protein’s structure and function are intimately connected, so information about a protein’s structure helps scientists understand how that protein works– or doesn’t work – such as in the context of disease mutations. This knowledge can help scientists design drugs to block or activate these proteins or even “engineer” new proteins to do new things.

 

There are lots of cool things that can be done with a protein’s structural information, but this information is hard to get! One way scientists can get it is through a technique called x-ray crystallography. Crystallography can provide detailed looks at proteins, but it requires proteins to crystallize, which they don’t like to do, so crystallographers usually have to screen through lots of conditions to find ones under which the proteins will form crystals. This can be very tedious, so Janet Newman is working to teach computers to recognize ordered crystals from aggregated protein clumps and other things. She has a software called Cinder, which she describes as crystallography tinder – crystallographers can look at their crystal trays, swipe right for crystals, left for clear, up for precipitate and down for other!

 

And you can help her! She’s crowdsourcing this “scoring” training. You can download the free Cinder app and classify crystal data sets (it’s easy to do and there’s also a training set called Cinder Kinder you can learn on). https://research.csiro.au/crystal/user-guide/c3-cinder/ 

 

Newman works at Australia’s Commonwealth Scientific and Industrial Research Organisation (CSIRO), where she set up and runs the CSIRO Collaborative Crystallisation Centre (C3).

 

Looking at so many protein structures, she’s made some surprising discoveries – such as finding that a bacteria-fighting protein in platypuses’ milk has a fold never seen before (they named it the Shirley Temple fold because of its “ringlets”). This knowledge could help scientists combat bacterial resistance.

 

Last month, she was at CSHL to help teach the x-ray crystallography course, and I had the privilege of learning directly from her! (and can confirm that she’s incredibly nice as well as knowledgeable!)

Photo: CSIRO

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