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Structural biology at Brookhaven National Lab

[Brookhaven lab]New facility for Structural Biology at Brookhaven Natl. Lab.
A new wing is being added to the National Synchrotron Light Source (NSLS) at BNL with laboratory space for structural biology. The expansion, which is being funded by the US Dept. of Energy, should be completed in late summer 1994 and will provide individual enclosed laboratory space for each participating research team at the NSLS.

The present plan, shown in the figure, includes space for each beamline in the arc of the ring subtended by the addition. The two structural biology beamlines in that arc arc X8C, from the Argonne Laboratory, and the X9A/B from the U. of PA. The Laue-diffraction effort focused on X25 and X26-C will have space, and the BNL Biology beamlines at X12 will use and oversee the cold room adjacent to the general laboratory. All other biological beamlines, including the BNL Biology X-ray scattering and VUV spectroscopy stations, the Howard Hughes beamline, and the SUNY/IBM/LBL X-ray microscope will have lab space adjacent to their beamlines within the existing NSLS building.

The macromolecular crystallography beamline at the High Flux Beam Reactor (HFBR) underwent modifications to increase the efficiency of data collection by a factor of 4 to 6, including the installation of a second detector. In addition, installation of MADnes, the Munich Area Detector data acquisition and reduction package, provides a user-friendly interface to the experiment and an efficient means for evaluating the data collection in real time. A cryogenic system that can reach 80 K provides H3A with the ability to perform temperature-dependent studies aimed at distinguishing static disorder from physiologically relevant dynamic effects in the motions of a macromolecule and its interaction with its solvent environment.

Hardware improvements have been made on the Small-Angle Neutron Scattering HFBR Beamline H9B. Neutron guides to extend the white beam path and eliminate 'beam dilutions' should increase flux and simplify camera alignment. It will also be possible to consider a curved primary path, and the installation of a satellite instrument.

Prior to Mar. 1993, 38 different research groups paid a total of 121 visits to NSLS Beamline X12C for Macromolecular X-ray Crystallography. The structure of GH5, the globular fragment of historic H5 was determined by the multiwavelength anomalous dispersion (MAD) method. A storage-phosphor     based diffractometer (MAR Co., Germany) with a 300 mm diameter screen and a K-axis goniometer was installed. Computer enhancement and installation of a cryogenic system is underway. The Time-Resolved X-Ray Diffraction Beamline X12B which was upgraded in 1992 are under nearly continuous use, with heavy emphasis on the dynamics of phase separation or ordering phenomena in polymers. Increased use of the unique data acquisition capabilities of X12B by the biological community is sought. Beamline X4, sponsored by Howard Hughes Medical Inst. is making use of X-ray storage phosphors used in the 'rotation photography' mode for data collection. The apparatus has been optimized for the MAD method. Beamline X8C, sponsored in part by Argonne National Lab., has introduced a two-dimensional X-ray detector for macromolecular crystallography. It is based on an X-ray phosphor viewed ultimately by a charge-coupled device electronic imager.

The individuals responsible for various applications are M. Capel, Time-Resolved X-Ray Diffraction, 516-282-2792, e-mail: capcl@criml2b.; R. Korszun, Neutron Crystallography, 516-282-7306, e-mail:; D. Schneider, Neutron Small Angle Scattering, 516-282-3423, e-mail:; and R.M. Sweet, X-Ray Crystallography, 516-282-3401, e-mail:

For further information and to be added to the mailing list for the BNL Structural Biology Newsletter contact Ann Emrick, Biology User Coordinator, 516-Tel.: 282-5756, e-mail: emrick@

Taken from BNL Structural Biology Newsletter (Mar. 1993).