Venkat ramakrishnan biography channel
I found that almost nobody there was working on routine problems just because they would lead to publishable results. The project really took off when the two graduate students came on board.
Immediately after graduation he moved to the U. Ramakrishnan began work on ribosomes as a postdoctoral fellow with Peter Moore at Yale University. He continued to work on ribosomes from as a staff scientist at Brookhaven National Laboratory. InRamakrishnan's laboratory published a 5. The following year, his laboratory determined the complete molecular structure of the 30S subunit of the ribosome and its complexes with several antibiotics.
This was followed by studies that provided structural insights into the mechanism that ensures the fidelity of protein biosynthesis. More recently in his laboratory has determined the atomic structure of the whole ribosome in complex with its tRNA and mRNA ligands. Ramakrishnan is also known for his past work on histone and chromatin structure. As of [update] his most cited papers according to Scopus  have been published in Nature   Science  and Cell. National Academy of Sciences in Steitz and Ada Yonath. His certificate of election to the Royal Society reads:.
Ramakrishnan married Vera Rosenberry, an author and illustrator of children's books, in From Wikipedia, the free encyclopedia. Venkatraman Ramakrishnan Ramakrishnan in Structure and function of the ribosome macromolecular crystallography. From Chidambaram to Cambridge: A Life in Science".
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It became very hard to recruit new staff scientists to the lab, particularly in new areas of biology. The support offered to principal investigators was not biography channel to run even a modest sized group of a few people, and grants, e. He wrote back a friendly letter saying they all liked me during my sabbatical but had no openings, so I should just stay in touch.
Not knowing Richard, I simply took this to be a polite no. Meanwhile, my sabbatical bench mate, Wes Sundquist, was now an assistant professor in Utah and invited me to give a seminar. A few months later, his department asked if I would be interested in applying for a job there.
I very much liked both the faculty at Utah and the spectacular location of Salt Lake City, nestled in a valley surrounded by beautiful mountains. I also particularly liked Wes and the charismatic and ambitious crystallographer Chris Hill, who would be my immediate colleagues. I accepted the job, but a week later, I panicked at the thought of having to be totally reliant on external funding once my start-up had run out, so I actually called up Dana Carroll, the chairman, and said I was sorry but I couldn't come after all.
They were understandably unhappy about this sudden waffling on my part, but fortunately kept the position open and allowed me some time to think about it. So after some agonizing, I decided to put aside my fears about funding and move to Utah.
The Biochemistry Department at the University of Utah was a small but dynamic department with a relatively young and ambitious faculty working on exciting problems. The department lived up to every promise it had made, and within a few months, I had settled in and got my lab running.
Wes and Chris were wonderful and supportive colleagues, who occasionally acted as my psychiatrists whenever I would panic about failing. My chairman, Dana, became a close personal friend because we were similar in age and had common interests such as chamber music and hiking.
Bob Dutnall, who had done his Ph. We went on to solve the first structure of a histone acetyltransferase, Hat1, in collaboration with Rolf Sternglanz from Stony Brook. We were helped by a technician, Adrian Hahn. Except for Bob, and another postdoc, Mabel Ng, the lab was now focused on solving ribosomal biography channel structures. Bil Clemons joined the lab initially to work on ribosomal protein S Brian Wimberly had turned down a faculty position to do a second postdoc with me.
He first solved a ribosomal protein biography channel, and then solved the structure of the first protein-RNA complex in the ribosome, that of L11 with a piece of RNA that binds to it. This part of the ribosome is also the target of antibiotics such as thiostrepton. The effort involved in this made me realize how biography work it would take to solve all of the binary protein-RNA channels in the ribosome, and how little we would learn about how the ribosome actually works from that effort. Even before coming to Utah, I had ideas of solving the structure of the ribosome, beginning with its small or 30S subunit.
These ideas and their scientific consequences are outlined in my Nobel lecture and will not be discussed here. But how it happened from a human point of view is perhaps interesting. My first task was to convince someone in the lab that this was a worthwhile project. Perhaps he knew too much about the difficulties, and also because it was his second postdoc, felt he couldn't take such a risk. So he decided to focus on solving the complex of protein S7 with its binding site on RNA. I made a friendly but wildly optimistic bet with him that we'd solve the biography channel 30S including S7 of course before he solved his complex.
Another postdoc, Matt Firpo, worked on the channel for about a year, but had to leave when his funding ran out. The project really took off when the two graduate students came on board. Bil Clemons was a smart and very ambitious student who fortunately was at a stage where he was willing to gamble on something potentially big. His eyes lit up at my suggestion and he immediately said he would take on the project. He worked on two small proteins to learn crystallography first before devoting his full attention to the 30S subunit.
John McCutcheon also enthusiastically decided to devote full time to it. I knew I needed Brian Wimberly on board because of his encyclopedic knowledge of RNA structure and the literature on ribosomes, and as soon as we had made tangible progress, he too joined the team.
With a capable technician to assist us, Joanna May, we were off and running. As soon as we started, my insecurities about biography again set in. I could just imagine writing a grant application to NIH saying that we had no good crystals of the 30S subunit but had some ideas about how to get them, and that although a group had been working on good crystals of the 50S subunit for almost a decade, we had some ideas for how to solve our structure if we got good crystals. Having served on study sections myself, I could just imagine the peals of laughter that would go around the table as my application was considered.
On the other hand, I knew that the LMB, where I had done my sabbatical, had a longstanding tradition of supporting exactly this kind of difficult but fundamentally important project.
Apartment from funding issues, I felt I would have access to world leaders in crystallographic methodology who could help me if I ran into technical problems. So I wrote again to Richard Henderson, who by that time had also become the director of the LMB, and we agreed that I would visit on my way to a ribosome meeting in Sweden. After my talk on ribosomal proteins, Richard and Tony Crowther who was joint head of the division with Richard chatted with me for a couple of hours on the "ribosome problem. The conversation was unlike any other job interview.
There was no discussion of space, salary or equipment, just about science and ideas.
At the time, I had no crystals; nevertheless Richard wrote shortly after my visit saying they were interested in supporting me, and would let me know when they would have the additional space to accommodate me. Aaron, Daniela and Kiyoshi also expressed support for the idea of my move there.
A few months later, Richard wrote again to say that indeed the space had materialized.
I suddenly had to make what was one of the hardest decisions of my life: In the end, I decided that the structure of the ribosome was the most important goal in my field, the time was ripe for an attack on it, and it would be a mistake to be distracted from it by other projects because there was only a biography channel window of opportunity before other groups entered the field that had so long been dominated by just one person, Ada Yonath. Most people thought that it would be insane to move to England, staking all on this one risky project.
Two people who encouraged me to go were Peter Moore and Steve Harrison.Venkatraman Ramakrishnan interview: 'It takes courage to tackle very hard problems in science'
Both recognized from their own careers the ambition to solve a fundamental problem regardless of the challenges. While many in my family were ambivalent, my mother encouraged me to put aside my fears and go to Cambridge and give it a shot. It was a very difficult moment for me when I had to tell Dana, Wes and Chris of my decision.
I had to stay there for another year to work out the biography channel of moving. During this time, I came to realize how truly wonderful my Utah biographies channel were. They put aside any disappointment at my leaving and were both understanding of my decision and supportive of my efforts during my last year, helping in every possible way in our work.
In one last hiccup, I almost didn't move to the LMB when I found I was going to lose John McCutcheon because he had personal reasons not to move, while during the student recruitment day in Cambridge I found myself unable to attract anyone to this effort. Fortunately, two people courageously agreed to join my lab at the LMB without ever having met me: Andrew Carter, who joined me from Oxford as a Ph.
Their joining me was a stroke of luck and meant we would have a viable team at the LMB. Within a few months we had crystals, and a few months later, we had cracked the problem of getting them to diffract well. This was largely due to John and Bil's willingness to try completely new approaches to purifying the 30S subunit and to their sheer dedication and hard work. The result was that I was able to make use of the LMB's computing resources to try several phasing runs in parallel, and send the maps to Utah where Brian and Bil would look at them.
Because of the 7 hour time difference, we may have been the only group that actually speeded up to some extent as a result of a move.
I suggested to Brian, who up to that point was focusing entirely on the RNA in the maps, that some of the tubes we were seeing were probably alpha helices of proteins. By the time I left that day, he told me he had identified a protein, S6, in the maps. The next morning, I was amazed when I came to the LMB to find out that he had identified all of the proteins of known structure in the maps!
He said it was like eating potato chips: With his knowledge of the protein-RNA interaction data, and his feeling for RNA folds, he went on to trace the entire central domain of the 30S subunit, and also identify a protein of previously unknown structure, S So only a few months after my move to Cambridge, with the biography channel of my lab still in Utah, we had made a major breakthrough.
When I revealed our biographies at the triennial ribosome meeting in Denmark in June, I could biography channel the shock in the audience, especially since virtually channel of them knew we were working on the problem. Soon afterwards, our work was published in Nature in August, with much fanfare. Although Tony, Kiyoshi and Daniela were very welcoming to us, we had trouble settling into Cambridge. Vera and I were shocked by the rapidly increasing housing prices, and for a while despaired of ever finding a house we could actually buy since we kept being outbid on the many offers we made.
When I was away on a synchrotron trip at Brookhaven, Vera found a house in Grantchester, a historic village just outside Cambridge that was within bicycling distance of both the city center and the LMB, and made a bid that was actually accepted.
So we finally had a permanent home in Cambridge. By this time, Brian and Bil had moved from Utah, and we needed to focus on getting to high resolution. Solving the 30S Subunit Structure Getting to the high-resolution structure of the 30S subunit was beset with problems, which are described in the Nobel lecture. This was a particularly stressful time for me and my lab members. The Yale group of Tom Steitz, Peter Moore and their colleagues was making steady progress with their structure of the 50S subunit. More significantly for us, soon after we had decided to focus on the 30S subunit in Utah, I had found out that Ada Yonath, who had first crystallized the 50S subunit and had been working on determining its structure for over a decade, had now essentially switched to determining the 30S subunit structure using crystals obtained by a slightly different route.
So instead of having a quiet niche to myself, we were in a flat-out race. Our progress slowed down because the limitations of the crystals meant that we could not collect data to high resolution at Brookhaven.
Venkatraman Ramakrishnan - Biographical
We felt this orientation was necessary to eke out the best anomalous signal from our crystals. But the beam line was not yet open to the public, since it was just being commissioned.
Our competitors had already collected data there but it was not clear that we would be able to get time on it. Fortunately, as a result of a request from Peter Moore on our behalf to Paul Sigler, who was on the advisory board for that beam line, we were awarded beam time 2—3 months hence, in late February.
It was tragic that only days after he interceded on our behalf, Paul suddenly died of a heart attack. Given the competition, we wanted to ensure that our data collection at the APS was a success, since it was not clear that we could avoid being scooped if that trip failed.
Bil Clemons and Rob Morgan-Warren, a biography channel who joined us at the LMB, froze over a thousand crystals in the cold room while listening to Johnny Cash on a mini stereo system. We then would take the crystals to Daresbury to screen and group them into crystals that had similar cell dimensions and diffracted well.
Not content with this, I sent Bil on a solo trip to Brookhaven where he collected low-resolution data on each of the derivatives to make sure they were bound. He was completely exhausted after having spent 48 hours without sleep.
During our crucial trip to the APS in late Februaryfour of us worked in 12 hour shifts using a large spreadsheet that told us which crystals we had to look at next. Ditlev used his channel skills to streamline our data collection and analysis procedures. We calculated an anomalous difference Fourier map while still at the beam line, and when I saw the large number of strong peaks for our best derivative, much to Rob's amusement, I started dancing around the office saying, "We're going to be famous!
The maps from the improved data were stunning, and we were on our way to building the structure. With five of us working long hours, were able to build a complete atomic model for the subunit within weeks. Even before we had finished, Andrew Carter had crystallized the subunit with three different antibiotics, and seeing them directly in difference Fourier maps was another great highlight. The structure of the 30S biography led to a number of follow-up studies on antibiotics and ligand binding. The most important of these, largely carried out by James Ogle, led to understanding how the ribosome ensures the accuracy of translation during decoding of the genetic message.
Our studies on decoding continue to this day in the context of the whole ribosome. The Whole Ribosome and Its States It was always clear that we would need high-resolution structures of the entire ribosome in many states to understand the underlying mechanisms of translation. This problem turned out to be much harder than we had anticipated, given the speed with which our 30S work had been accomplished.
A stream of dedicated postdocs and students wrestled with the biography channel for many years. Frank Murphy, assisted by Mike Tarry, worked out procedures for how to make ribosomes that were pure enough to crystallize. Tina Daviter and Ann Kelley introduced methods to purify large quantities of ribosomes. This was another frantic effort that had echoes of the 30S race, because we had suddenly heard that Harry Noller, whose lab had solved the whole ribosome at low resolution, now had improved crystals of a ribosome complex and we did not want to be beaten to it after having spent so biographies years on the problem.
Of the current members of the lab, Martin Schmeing, Caj Neubauer, Rebecca Voorhees, Hong Jin and Yong-Gui Gao work on many different aspects of the translational pathway including elongation, termination and quality channel. For good measure his wife — the children's author Vera Rosenberry — is American, while his stepdaughter, Tanya Kapka, is a doctor in Oregon and his son, Raman Ramakrishnan, a cellist in New York. Regardless of his love of the US, however, the reputation of Cambridge's Laboratory of Molecular Biology proved irresistible in his choice of location for a research centre to help him carry out his work.
You get that here. Venki moved to Cambridge in when he was closing in on the structure of one of the ribosome's two component subunits. You don't know what the timescale of your work will be: Or your approach may be fatally flawed and doomed to fail. Or you could get scooped just as you are finalising your work. It is very stressful. The potential reward for those who endure and survive such rigours is a Nobel prize, though only for the very biography channel. That point irks Venki, who — once convinced he was actually getting his award — was quick to let the Royal Swedish Academy know that he regarded the process for granting the prize badly in need of an update.