Structural Biology and Synchrotron Radiation:
Evaluation of Resources and Needs

Report of BioSync -- The Structural Biology Synchrotron Users Organization

1997

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Cover illustration:

In the center of the front cover is a protein crystal. To the left is a structural model of cytochrome bc1, an integral-membrane electron-transfer complex of bovine mitochondria. Diffraction data from synchrotron sources, essential to the structure determination, were measured at NSLS, SSRL, ESRF and CHESS. The top of the complex is in the mitochondrial intermembrane space, the center spans the membrane, and the bottom is in the mitochondrial matrix. The complex is a 496-kDa dimer of eleven different protein subunits. Courtesy of D. Xia and J. Deisenhofer, University of Texas Southwestern Medical Center.

To the right is electron density at ultra-high resolution (0.78 Å) superimposed on the refined model of a Pro-His dipeptide in B. lentus subtilisin. Diffraction data were measured at SSRL. Courtesy of R. Bott, Genencor International, and P. Kuhn, SSRL.

These images are superimposed on a diffraction pattern to 2.1 Å for carbamoyl phosphate synthetase, a complex enzyme that synthesizes carbamoyl phosphate from bicarbonate, glutamine and two molecules of Mg-ATP in four catalytic steps using three distinct active sites. High-resolution data were measured at SSRL from crystals of the 650-kDa tetrameric enzyme. Courtesy of J. Thoden, H. Holden and I. Rayment, University of Wisconsin - Madison.