Asmit Bhowmick

Project Scientist

Molecular Biophysics and Integrated Bioimaging

Bioenergetics

Building: 33, Room 349
Mail Stop: 33R0345
abhowmick@lbl.gov

Research Interests

Unravelling the relationship between structure, dynamics and function of enzymes using
- Time-resolved structural studies at X-ray free-electron lasers (XFEL)
- Simulating biological systems using Molecular Dynamics/Quantum mechanical methods
X-ray crystallography data analysis – developing new methods for active sites of metalloenzymes
Current systems of interest include Photosystem II, a multi-subunit membrane enzyme catalyzing the water oxidation reaction.

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Crystallography for the Misfit Crystals

January 19, 2022

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.

New Technique Gets the Drop On Enzyme Reactions

October 21, 2021

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.

New Refinement Technique Promises Greater Protein Structure Accuracy

December 21, 2020

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.

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