Being part of the structural biology lab, I always heard that crystallography is more art than science from my fellow researchers. The art here is quite different and yet similar to the art on paper. Several shades and tints of colours give us various forms and expressions on paper, which goes for protein crystallography. The initial days were fascinating to play around with the proteins of other lab mates and learning techniques. Then I found my PhD project protein — Myosin-1b from Entamoeba histolytica. I devoted all my energy and hands — on skills to work on it as a pioneer to establish a different protein expression system than a conventional bacterial system. I trained myself at Indian Institute of Science, Bangalore and returned to set up the same at my parent organization, Jawaharlal Nehru University. Uncountable trials were done for almost a year, but I was unsuccessful in getting my protein. The demotivation captured me and others too for the expression of this protein in my lab. My supervisor asked me to shift to another set of proteins — p21-activated kinases (PAKs) from the same organism. During these struggling phases of trial and error, almost two years passed! I started to work on PAK proteins but somehow internally couldn’t leave the love for my first protein — Myosin-1b. I decided not to give up on it, unless I found some concrete reason to leave it. While reading the IndiaBioscience newsletter of June 2018, I saw a short-term fellowship named ​“Newton Bhabha” funded by the British Council and Indian partners — Department of Science and Technology and Department of Biotechnology. I never imagined that one day I could be part of it. I checked all the basic details immediately and started working on Newton Bhabha’s application. I approached scientists in UK universities and institutes who worked on cytoskeleton proteins. I was exhilarated after my confirmation from John Kendrick John, Emeritus Professor at MRC — LMB and Folma Buss, Professor, CIMR Cambridge. I would like to make a special mention here of the assistance provided by the UK HE international unit for contacting scientists. They rejuvenated my energy and hope for Myosin-1b in the first online interaction to discuss the project. I could not morph my expression of getting tired while working on a lengthy application, and it seemed like they wanted to enter my brain. From the first question that asked, ​“please give a summary in plain English of your proposed PhD placement within the context of your PhD. This should be a statement for a non-specialist audience about the research of your PhD project and the purpose of your place visit”, the application form was unique. The result was expected after four months, and I was not sure whether I would make it or not. My attachment to the protein led me to have two-three online discussions, and I prepared all the initial material for the protein expression. 

I got selected for the fellowship and landed in Cambridge University for my work. 

A drastic difference in work culture and guidance made me more scientifically sound and hopeful. As we already knew, Myosin-1b behaves slightly differently; we were mentally prepared for failures on our way. John and Chris consistently guided my benchwork, we troubleshooted the problems together, and finally, I got the protein. However, it was less than the required amount for crystallization, but I felt satisfaction when I saw Myosin-1b on SDS-PAGE, a technique commonly used to visualize proteins. I cherish all the cake parties and lab meetings by Folma. I think six months rather than four months would have been more fruitful. I have been part of the 36-member family of the Newton Bhabha fellows of that year from different research areas. I helped two-three applicants who contacted me for guidance in the application form, and one got selected. It feels worthy when you can pass it on to coming generations.