He shares the prize with Thomas A Steitz of Yale University and Ada E Yonath of the Weizmann Institute of Science in Israel.
After the news reached him, Dr Ramakrishnan said: "I have to say that I am deeply indebted to all of the brilliant associates, students and post doctors who worked in my lab as science is a highly collaborative enterprise. The MRC Laboratory of Molecular Biology and the University of Utah supported this work and the collegiate atmosphere there made it all possible. The idea of supporting long term basic research like that at LMB does lead to breakthroughs, the ribosome is already starting to show its medical importance."
The Indian-born scientis, aged 57, is the senior scientist and group leader at the Structural Studies Division of the MRC Laboratory of Molecular Biology in Cambridge, England.
Sir Leszek Borysiewicz, of the Medical Research Council Chief Executive, said: "We are absolutely delighted that Dr Ramakrishnan's work has been recognised with the 2009 Nobel Prize for Chemistry. Venki's award is the Medical Research Council's 29th Nobel Prize and is a reflection of the excellent work that our scientists do. The MRC is committed to long-term support of the difficult areas of basic science as exemplified by Venki's success. It is only on the back of such discoveries that we can continue to drive translation into benefits for human health."
The three have won the Nobel Prize for atom-by-atom mapping of the protein-making factories within cells -- a feat that has spurred the development of antibiotics.
Ribosomes produce proteins, which in turn control the chemistry in all living organisms. The ribosome is found in all living cells, including those of bacteria. Human and bacterial ribosomes are slightly different, making the ribosome a good target for antibiotic therapy that works by blocking the bacterium's ability to make the proteins it needs to function.
Ramakrishnan, Steitz and Yonath demonstrated what the ribosome looks like and how it functions at an atomic level using a visualisation method called X-ray crystallography to map the position of each of the hundreds of thousands of atoms that make up the ribosome.
Dr Ramakrishnan's basic research on the arrangement of atoms in the ribosome has allowed his team not only to gain detailed knowledge of how it contributes to protein production but also to see directly how antibiotics bind to specific pockets in the ribosome structure.
This could help researchers to design antibiotics to treat people who are infected with a bacterium that has developed antibiotic resistance, for example some of the strains of bacteria that cause tuberculosis. Better targeting of the bacterial ribosome should also help to avoid negative effects on human cells thereby reducing the side effects of taking antibiotics.