Harry Noller, the Sinsheimer Professor of Molecular Biology at the University of California, Santa Cruz, and his coauthors on a groundbreaking paper published last year have received a major award in recognition of their achievements. The American Association for the Advancement of Science (AAAS) has awarded them the Newcomb Cleveland Prize, which is given annually to the authors of an outstanding paper published in the association's journal Science.

The winning paper described in unprecedented detail the structure of the ribosome, a tiny molecular machine crucial to all forms of life. Ribosomes are the protein factories of all living cells. Noller's group used a technique called x-ray crystallography to obtain precise images of the ribosome's structure. It is the largest molecular structure ever solved by x-ray crystallography.

In addition to Noller, who directs UCSC's Center for Molecular Biology of RNA, the authors included Marat Yusupov and Gulnara Yusupova, a husband-and-wife team who were visiting researchers in Noller's lab and are now at the Institute of Genetics and Molecular and Cellular Biology in Strasbourg, France. The other coauthors and corecipients of the prize are Albion Baucom, a computer specialist in the RNA Center; postdoctoral researcher Kate Lieberman; Thomas Earnest at Lawrence Berkeley National Laboratory; and Jamie Cate, now a faculty member at UC Berkeley and formerly a postdoctoral fellow in Noller's lab.

The Newcomb Cleveland Prize, established in 1923 with funds donated by Newcomb Cleveland of New York City, is the oldest award given by AAAS. Winning papers are chosen for fundamental contributions to basic knowledge or technical achievements of far-reaching consequence.

A formal presentation of the prize will take place at an awards ceremony and luncheon on Saturday, February 16, at the AAAS annual meeting in Boston. Each of the recipients will receive a bronze medal, travel and hotel expenses to attend the meeting, and a share of the $5,000 prize.

Noller has been studying the ribosome for more than 30 years. Last year, he received the prestigious Lewis S. Rosenstiel Award for Distinguished Work in Basic Medical Science in recognition of his accomplishments.

Understanding the workings of the ribosome has practical significance because many antibiotics work by binding to and disrupting bacterial ribosomes. Ongoing research by Noller and others on the ribosome's structure may lead to the development of new and more effective antibiotics.

The prize-winning paper was initially published online in March 2001, and appeared in print in the May 4 issue of Science.

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