We asked our recent intern, Maryam Arab, what she thought about her 3 month placement with us.

Bee in lavender field

Maryam Arab

What are you studying (and where)?

I am a first year PhD student enrolled on the BBSRC funded Midlands Integrative Biosciences Training Partnership (MIBTP) programme at the University of Birmingham. My PhD project falls under the MIBTP theme of molecules, cells and systems, and I am looking at cross talk between tetraspanins, membrane proteins that organise a network of interactions at the cell surface, and cell junctions that link cells together.

How did you organise your internship here?

As part of the doctoral training programme, we are encouraged to complete an internship outside of the lab to provide additional skills and experience beyond academic work. I took this opportunity to learn more about scientific publishing. However, I also wanted an internship in an organisation that communicates science and emphasises the cultural role that science has to play in society. This led me to the Royal Society, and I identified Open Biology as a journal relevant to my interests. I contacted the Publishing Editor of the journal about the possibility of undertaking an internship, and we discussed a potential focus for the placement from there.

What have you learnt?

The internship has been a fantastic opportunity to learn about science publishing from a publisher perspective. I primarily supported editorial office staff with the processing of submitted manuscripts through peer-review, overseeing the peer review process, and searching for peer reviewers. However, I also worked on bigger on going projects, contributed blog posts and launched new content on social media. The varied responsibilities developed my science communication skills and ability to work across different levels of management. My improved understanding of publishing will be very useful when I am publishing articles in the future.

My improved understanding of publishing will be very useful when I am publishing articles in the future.

What’s been your favourite thing about working here?

Attending the monthly staff meetings allowed me to learn more about the work carried out by other departments of the Society. I got the opportunity to meet with a policy advisor from the Science Policy Centre that talked me through current projects and how they work with local and international government bodies. I also took advantage of being at The Royal Society and attended public events that exposed me to research areas outside of my own field. My highlight was the 2016 Croonian Lecture by Professor Enrico Coen CBE FRS.

Was it different to how you thought it was going to be?

Initially I was worried that an office based internship would be rather repetitive compared to the day-to-day variety lab work provides. However, I worked on additional projects alongside my key responsibilities and really enjoyed the varied nature of the work at Royal Society Publishing. Journal work also took me outside of the office, and I got the opportunity to attend the British Societies of Cell Biology and Developmental Biology spring meeting at the University of Warwick during the second week of my internship!

Is there something surprising you learnt about science publishing that you didn’t know before?

Science publishers take an active role in taking the wider community, not just scientists, beyond the peer reviewed research paper. Communicating the research to the general public in addition to academics on social media platforms and blogs encourages exchange and discussion of science. This reinforces the idea that we need evidence for scientific claims.

Do you have a favourite paper which published whilst you were here?

My favourite paper is a research article that presents the structure of the separase-securin complex from Caenorhabditis elegans (roundworm). The separse-securin complex is an essential regulator of chromosome segregation. However, very few structural studies have been carried out, as it is difficult to generate recombinant separase-securin complexes. Bachmann and colleagues successfully generated the recombinant separase-securin complex for electron microscopy studies. The model they obtained from their studies showed that the separase-securin complex possesses a “closed” shape. The structural work is accompanied by biochemical experiments, which aid with the interpretation of the structure of this essential protein complex.

Maryam recently completed her internship and is now back in the lab. We would like to thank her for all her help over the past few months. 

 

 

 

Authors

  • Ruth Milne

    Ruth Milne

    Editorial Coordinator