Interview, December 2017

Interview with Chemistry Laureate Richard Henderson on 6 December 2017 during the Nobel Week in Stockholm, Sweden.

Richard Henderson answers the following questions (the links below lead to clip on YouTube):
0:00 – What was the moment when you decided to pursue science?
2:44 – How was it to grow up in rural Scotland?
5:18 – Has hill walking and exploring fed into your science?
9:22 – How did you learn you had received the Nobel Prize?
14:16 – What has receiving the Nobel Prize meant to you?
15:24 – What impact has cryo-EM had in the world?
17:06 – What has been your invention’s greatest benefit to humankind?
21:48 – What is the power of the tea break in a scientific setting?
26:12 – What advice would you give to a young researcher?

Nobel Minds 2017

Telephone interview, October 2017

Interview transcript

Richard Henderson: Hello, Richard Henderson here.

Adam Smith: Oh hello. My name is Adam Smith calling from Nobelprize.org, the website of the Nobel Prize in Stockholm. Congratulations on the award of the Nobel Prize.

RH: Thank you very much.

AS: How did you hear the news?

RH: I’m at a meeting about cryo-EM in Leicester University so I’m just in the session listening to people speaking. So my phone rang in the meeting, and I had to go out of the room, the lecture room, to hear it. And by then the reception had been cut off a couple of times. But eventually after about five minutes I managed to get through and then I chatted to Gunnar von Heijne who I knew first, and then three other people from the Nobel Prize Committee. And then they told me that the Chemistry Prize was going to be awarded with Jacques Dubochet and Joachim Frank who of course I know very well, so I think that’s quite delightful really. Of course there were a few other people who also contributed. But I think all of us know the Nobel Prize awards are always, usually only to three people. So there are often one to two others who’ve made strong contributions who didn’t quite cross the threshold.

AS: The meeting is a wonderful environment to hear in because I imagine that everybody will be celebrating today.

RH: It’s quite a small meeting. There’s only sixty people or something.

AS: Nice for a celebration. You were the first to achieve atomic resolution of biomolecules with cryo-EM. What does it allow you to see? What detail can we now see that we couldn’t see before?

RH: I think the first structures of biological molecules were by x-ray crystallography back in 1959, 1960, with John Kendrew who had a Chemistry Nobel Prize for work on myoglobin and developing the x-ray methods. And since we’ve had over the last 50 years hundreds of… at least a hundred thousand structures done by x-ray crystallography, so in a way cryo-EM is just another method of finding out what the atomic structure, high-resolution structure, of your molecules are. But the difference is there are quite a lot of structures in biology that were resistant, were recalcitrant to the other methods, like x-ray crystallography or nuclear magnetic resonance spectroscopy. So it has opened up essentially a kind of new, previously unapproachable area of structural biology. And I think my original work was working on membrane proteins which we found difficult to crystallise. The real power has come from the images where you don’t need crystals, so you just take a picture, you look at it, you process it, you average structures, you get the… so it is a much more direct method than making crystals, getting diffraction plots and then figuring out what the diffraction plots mean. So I think it’s a direct method, easy to understand and much more general in its power and what you can use it for.

AS: Thank you. This is another Nobel Prize for the MRC-LMB for structure determination.

RH: [Laughs] Yes.

AS: It seems that its specialness continues. What is it that makes it such an extraordinary place?

RH: I think it’s got long-term support from the Medical Research Council. And actually this is the 105th year that the UK Medical Research Council has been supporting either medical, or biomedical, or biology-related-to-medicine structural work, and they’ve got a lot of experience in managing groups, units or institutes, and actually they’ve been quite bold in terms of supporting new ideas, and actually closing down other areas that have fulfilled their purpose. The MRC Molecular Biology Lab in Cambridge of course benefitted greatly from the people who founded it back in the 50s. So Max Perutz was the original first head, he called himself a chairman, and he was very good at recruiting people, allowing them to follow their own ideas in depth. And so that culture has permeated throughout the lab since it started, and that’s, I mean, there’ve been little gaps, but periodically there have been Nobel Prizes for all sorts of different things actually.

AS: Yes indeed.

RH: So it’s been a very successful lab. Obviously I went there as a student. I’ve been there for 51 years or something like that. So, you know, I’ve certainly absorbed the culture and helped to try and propagate it for the future.

AS: Well how nice to find such a good home. They say there’s a Nobel Laureate on every floor of the LMB and now they have another.

RH: [Laughs] Yes, quite a lot of them have retired now, so actually it’s good to have one or two new ones. And I actually partly retired.

AS: We very much look forward to welcoming you to Stockholm in December. Will you be coming?

RH: Oh yes, I’m sure I’ll be able to come, even if I’ve got another booking I’m sure I can change it.

AS: Once again, congratulations, and it was lovely to speak to you. Thank you.

RH: Many thanks then.

AS: Thank you, bye bye.

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