Bronte Johnstone

Coffee-fuelled research fellow in Structural Biology at @Bio21Institute @unimelb.

[Bronte Johnstone @bronteaj]

Cryo-EM was conducted at Ian Holmes Imaging Centre at Bio21 Institute with data collected by Hamish G Brown. Done with @Bio21Director, @michchris14, @Riya_Joseph_a, Craig Morton, @big_french_man and Rod Tweten and team.

[Bronte Johnstone @bronteaj]

Excited to share that our work on a family of pore-forming proteins is now live in @ScienceAdvances ! We show structural snapshots across the entire pore-forming pathway for a cholesterol-dependent cytolysin-like (CDCL) bicomponent system.

[Bronte Johnstone @bronteaj]

This work was part of my PhD at UniMelb and was my first foray into cryo-EM! Admittedly, learning the various steps of cryo-EM on proteoliposome samples felt like jumping in the deep end so I am very happy and proud for all to see how it worked out.

[Bronte Johnstone @bronteaj]

Definitely one of the coolest structures I'll ever work on! 🤩

[Bronte Johnstone @bronteaj]

Just in time for Christmas, our paper on the structure and evolution of baculoviruses is out! Excited to share some work I did at Monash in the @CoulibalyLab, with shout outs to co-authors @joshuamhardy and Jungmin, collaborators Mart and team and everyone else who contributed!

[Bronte Johnstone @bronteaj]

https://t.co/YnR8QELnKB

[Bronte Johnstone @bronteaj]

@Bio21Director This is only the start of our investigation into these novel bacterial toxins and their unique mechanism among pore-forming toxins, so watch this space!

[Bronte Johnstone @bronteaj]

See our latest work from the Tweten, Comstock and Parker @Bio21Director labs highlighting unique CDC-like bacterial toxins in Bacteroidetes that require proteolytic activation and form two-component pores via a mechanism reminiscent of the complement MAC to target other bacteria

[Bronte Johnstone @bronteaj]

@Bio21Director In addition, we identify an immunity protein much like the mammalian GPI-anchored CD59 that inhibits the MAC pore formation

[Bronte Johnstone @bronteaj]

@GeorgopoulouME @LorneProteins @PaulBindusmita @Saharnaz_Rafiee @Bio21Institute @CCeMMP Congratulations Marialena! Not surprised to hear you did an awesome job as always!

[Bronte Johnstone @bronteaj]

Tomorrow - my turn to share our work on novel pore-forming toxins. Come to session A013 if you are interested in bacterial toxins, pretty structures or both like we are!

[Bronte Johnstone @bronteaj]

Very excited to finally be at the start of IuCr2023! Opened today by @Bio21Director and loved hearing the history behind phasing methods that worked successfully for me during my PhD.

[Conall Mc Guinness @Mac__Aonghusa]

Nice review on the current questions around cholesterol dependent cytolysins in @iubmb_life from @bronteaj in the Parker lab @Bio21Institute that the @Mol_Machines group got to be a part of. https://t.co/LsllZaWq4E

[Bronte Johnstone @bronteaj]

@MohebaliNazanin Congratulations Nazanin! 🎉 Such a great talk today too! 😊

[Bronte Johnstone @bronteaj]

@SValimehr Congrats Sepideh! 🎉 such a great talk today and so much achieved - you should be super proud of yourself! 😊

[Bronte Johnstone @bronteaj]

My first ever conference was MPG as a fresh-faced Honours student, in awe of others. A few years on I feel very fortunate to be selected to present my work, and even more so to win an award, at the 2021 MPG meeting during the final year of my PhD. Thanks for a great meeting!

[Melbourne Protein Group @MelbProtein]

Congratulations to all the winners of the MPG meeting presentations. Thanks everyone, stay safe and look out for each other #MPG21online

[Bronte Johnstone @bronteaj]

The pore-forming toxin community has done a fabulous job at achieving crystal structures - although that meant a lot of reading was done in order write this chapter! Happy to see that some of my efforts during working from home in 2020 is now in-press!

[Dr Shane Huntington OAM @DrShaneRRR]

Here is a piece I wrote for all you PhD students trying to work during the Pandemic. Spread widely people.

https://t.co/bFLSTaIBjt

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