April 7-11, 2008

RapiData Celebrates 10 Years of Teaching Crystallography Skills

One of the most widely recognized courses at the National Synchrotron Light Source (NSLS) turned 10 this year. Since 1999, students from around the world have gathered at the NSLS every spring for RapiData, a weeklong crash course designed to introduce participants to the best and latest equipment and techniques for macromolecular x-ray crystallography. RapiData allows students to meet and learn from the leading developers of software in the crystallography field, and then to actually use NSLS beamlines to collect data. This year, 52 students attended the workshop, which was held from April 7-11.

Participants of the RapiData 2008 course

“Since its creation, nearly 500 students have attended this course, and we have constant requests to add more slots,” said Bob Sweet, who came up with the idea for RapiData and organized this year’s course along with Alex Soares and Sal Sclafani, all of Biology. “Many RapiData alumni have now blossomed into crystallography experts, and they continue to refer their less-experienced colleagues to BNL to learn the initial steps of this highly specialized area of interest. We regularly get graduate students of former RapiData students.”

The course is offered by BNL’s Biology and NSLS departments, and reflects an educational component of the PXRR (Macromolecular Crystallography Research Resource), funded jointly by the National Center for Research Resources – a branch of the National Institutes of Health – and the U.S. Department of Energy’s Office for Biological & Environmental Research.

X-ray crystallography allows scientists to determine the arrangement of atoms within a crystallized material based on the way x-ray light bounces off its electrons. This is especially important in determining protein structures, which are needed to establish a fundamental understanding of life processes and for developing drugs and treatments for disease.

leptospiral protein LIC10793

The course began with a daylong background session taught by Sweet, meant to refresh the knowledge of crystallography fundamentals for less-experienced students. The following two days were filled with lectures and tutorials taught by scientists from BNL, industry, academia, and other national labs. Next, the students were divided into groups and guided through a marathon, 60-hour data-collection session on six or more NSLS beamlines. At the same time, many tutorials were underway, run by the lecturers themselves. Half of the students brought their own specimens with the goal of solving the structure of a particular enzyme, while the other half observed and helped.

About five or six structures were solved during the course, each of which could be a publishable result, Sweet said. During the data-collection portion of the course, the students gathered each afternoon to discuss their results and produced mini lectures about their data and scientific subject.

“It’s always really exciting to watch the students’ skills develop throughout the week,” Soares said. “Many of them come here with little or no experience in crystallography and they leave knowing how to obtain and process real data, as well as how to locate and fix problems as they arise. That’s the advantage of having such a hands-on program.”

In addition to the DOE and NIH funding, a special grant was provided by the International Union for Crystallography to assist four Latin American students in attending the course. Additional support was provided by Brookhaven Science Associates, the NSLS, and several equipment vendors and drug companies.

The Revolving Ribbon Logo

Some might have noticed that the RapiData logo, which shows up on the course website and on participants’ T-shirts, changes every year. The organizers select a different “ribbon diagram” – one of the most popular ways to depict protein structures – based on an interesting structure from the previous year, often one solved during the course. The logo for RapiData2008, which resembles the profile of a fish, was solved at the 2007 course by a group from the Brazilian Synchrotron Light Laboratory. This protein is found in the bacteria that causes Leptospirosis, a disease that affects humans and a wide range of animals.