Calcium channel blockers are widely prescribed for heart and blood-vessel diseases. With the help of the high-intensity x-ray beams and remotely controlled robots at the Advanced Light Source (ALS), two groups of scientists from University of Washington have revealed, at atomic resolution, how two different classes of calcium channel blocker drugs produce their therapeutic effects. The researchers took advantage of the remotely controllable robot automounter available in the Berkeley Center for Structural Biology at the ALS to screen a large number of crystals for the best diffraction. The tunable x-ray source also allowed them to collect anomalous diffraction data at Beamlines 8.2.1 and 8.2.2 with bromine-incorporated drugs, which was critical for locating the drug molecules in the crystal. The results pave the way for optimizing these classic compounds for safer and more reliable pharmaceutical applications. Read the ALS Science Highlight.
In their Nano Letters paper released August 23, 2016, a research team led by Danielle Tullman-Ercek, biologist faculty scientist in Molecular Biophysics and Integrated Bioimaging, described a new size selection method for virus-like particle assembly using chromatography. Their work has important implications for virus evolution theory, multi-protein assembly behavior, and protein-based nanomaterial development.
Based on a beamstop technology licensed from Berkeley Lab earlier this year, MiTeGen LLC has launched the Sentinel™ Real-time Intensity Monitoring Beamstop System for X-ray beamlines. The device improves data collection from X-ray scattering experiments conducted by researchers seeking potential treatments for cancer, AIDS, Ebola, and other diseases.
The Compact Dynamic Beamstop technology developed by Diane Bryant and Simon Morton (pictured) at the Berkeley Center for Structural Biology and licensed by MiTeGen was named a finalist in the 2016 R&D 100 Awards earlier this month, along with six other Berkeley Lab technologies and one multi-lab collaborative effort. Recently, the developers and MiTeGen staff presented the device at the 2016 American Crystallographic Association meeting in Denver.
Naturally occurring proteins—chains of amino acids that fold into functional, three-dimensional shapes—are believed to represent just a small fraction of the universe of all possible permutations of amino-acid sequences and folds. How can we begin to systematically sift through those permutations to find and engineer from scratch (de novo) proteins with the characteristics desired for medical, environmental, and industrial purposes? To address this question, a team led by researchers from the Institute for Protein Design at the University of Washington have published a landmark study that used both protein crystallography (Beamlines 8.2.1 in the Berkeley Center for Structural Biology and 8.3.1) and small-angle x-ray scattering (SAXS; SIBYLS Beamline) at the ALS to validate the computationally designed structures of novel proteins with repeated motifs. The results show that the protein-folding universe is far larger than realized, opening up a wide array of new possibilities for biomolecular engineering. Read the ALS Science Highlight.