Brookhaven National Laboratory
Life Science Biomedical Technology Research (LSBR) at the National Synchrotron Light Source-II
The Life Science Biomedical Technology Research (LSBR) program at the National Synchrotron Light Source II focuses primarily on two areas of scientific, and technological research:
- macromolecular crystallography (MC)
- small-angle X-ray scattering/diffraction (XS)
Funded by DOE-BER and NIH-NIGMS the LSBR operates two macromolecular crystallography beam lines, 17ID-1 (AMX) and 17ID-2 (FMX), and one scattering beam line, 16ID (LIX). By partnering with other NSLS-II beamlines the resource offers complementary capabilities to its user base. These synergistic partnerships allow visiting researchers to probe their samples by spectroscopy from the infrared to hard X-ray range (EXAFS, XANES, IR) including microspectroscopy imaging and soft X-ray imaging.
The LSBR resource is located at the National Synchrotron Light Source II (NSLS-II), a 3 GeV storage ring designed to deliver photons with high brightness in the 2 keV to 10 keV energy range and a spectral flux density expected to exceed 1015ph/s/0.1%BW in all spectral ranges when operation reaches its design parameters. A DOE-funded national research facility, NSLS-II, at Brookhaven National Laboratory, Upton, New York, is available to all researchers in academia, industry, and other government Laboratories.
Macromolecular Crystallography allows for the three-dimensional structure determination of macromolecules proteins, DNA, RNA or assemblies such as viruses and ribosomes. Understanding molecular interactions, enzyme catalysis reactions, the action of drugs and disease mechanisms is essential to a large ensemble of subjects leading to improved agricultural practices, increased food supplies, energy sustainability, disease control and eradication to name a few.
17ID-1 the Automated Macromolecular Crystallography (AMX) beam line was developed to address those problems in need of efficient data collection on a vast number of samples. The beam line is well suited for biological structure determination of complexes in large unit cells, drug discovery explorations and the survey by diffraction of specimen at room temperature. Expected to deliver a flux of ~1013 ph/s at 1 Å into a 4 – 100 μm spot, AMX covers an energy range from 5 – 18 keV. Still under commissioning AMX is expected to be fully operational in 2018 offering the research community remote operation fast automated crystal screening assisted by crystallographic decision making software.
17ID-2 the Frontier Microfocusing Macromolecular Crystallography (FMX) beam line can support a broad range of structural determination methods from serial crystallography on micron-sized crystals, to resolving macromolecular complexes in large unit cells, to rapid sample screening and data collection of crystals in crystallization trays.
The high flux ~5×1012 ph/s at 1 Å delivered into a 1 – 50 μm spot, the wide energy range from 5 – 30 keV and a 100nm sphere of confusion allows makes the study of complex and difficult strcutures. The increased interest in the functional mechanisms of hierarchical complex systems of the biological molecules saw a growing interest in solution scattering methods. These methods are ideally positioned to monitor a broad range of interactions simultaneously elucidating structural applications at different levels.
16ID the High-brightness X-ray Scattering for Life Sciences (LiX) supports experiments in two scientific areas: (1) high throughput biomolecular solution scattering and solution scattering with in-line size exclusion chromatography, (2) scattering based scanning probe imaging of biological tissues.
Covering an energy range from 2.18 – 18 keV, provides variable beam sizes from 1 micron to a fraction of 1 mm. Equipped with 3 Pilatus detectors LIX covers a wide range of scattering vectors. Development is also in progress for time-resolved solution scattering using flow mixers, to reduce sample volume in static solution scattering and for scattering measurements on single- and multi-layered lipid membrane structures.