Nicholas Sauter, a computer senior scientist in the Molecular Biophysics and Integrated Bioimaging (MBIB) Division, is co-leading a team working to provide a better way for scientists to study the structures of the many materials that don’t form tidy single crystals. Their new technique, called small-molecule serial femtosecond X-ray crystallography, or smSFX, supercharges traditional crystallography with the addition of custom-built image processing algorithms and an X-ray free electron laser (XFEL). In a paper published in Nature, the team demonstrated proof-of-principle for smSFX and reported the previously unknown structures of two metal-organic materials known as chacogenolates.
A team of scientists, including many in the Molecular Biophysics and Integrated Bioimaging Division, uncovered new details about the reaction that powers photosynthesis. Understanding this reaction could lead to world-changing advances in technology, medicine, or energy––and also gives insight into how the enzyme photosystem II produces the oxygen we breathe. Their latest work was recently published in Nature Communications and two of the authors, Vittal Yachandra and Philipp Simon, spoke with Strategic Communications about that, shooting stuff with lasers, and why they chose this field of research.
As part of an international collaboration, researchers at Lawrence Berkeley National Laboratory (Berkeley Lab), the Diamond Light Source synchrotron facility, and Oxford and Bristol Universities in England have developed a novel sample delivery system that expands the limited toolkit for performing dynamic structural biology studies of enzyme catalysis, which have so far mostly been limited to a small number of light-driven enzymes.
Numerous Biosciences Area personnel are among the 2021 Berkeley Lab Director’s Awards honorees. This annual program recognizes outstanding contributions by employees to all facets of Lab activities. A complete list of winners can be found here. The 10th annual Director’s Awards ceremony will take place on November 18 at noon.
X-ray free-electron lasers (XFELs) came into use in 2010 for protein crystallography, allowing scientists to study fully hydrated specimens at room temperature without radiation damage. Researchers have developed many new experimental and computational techniques to optimize the technology and draw the most accurate picture of proteins from crystals. Now scientists in the Molecular Biophysics and Integrated Bioimaging (MBIB) Division have developed a new program, diffBragg, which can process every pixel collected from an XFEL for a protein structure independently. In a recent IUCrJ paper, the team led by MBIB Senior Scientist Nicholas Sauter proposed a new processing framework for more accurate determination of protein structures.