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10.1128/mBio.01242-21

Using single-particle cryoelectron microscopy (cryo-EM) and biochemical assays, we demonstrate that SAMase performs its function by not only degrading SAM but also by interacting with and efficiently inhibiting the host’s methionine S-adenosyltransferase (MAT), the enzyme that produces SAM.

SAMase of Bacteriophage T3 Inactivates Escherichia coli’s Methionine S-Adenosyltransferase by Forming Heteropolymers

10.1016/j.str.2021.06.004

Here, we reconstitute the mouse Ptc1 into lipid nanodiscs and determine its structure using single-particle cryoelectron microscopy.

Cryo-EM study of patched in lipid nanodisc suggests a structural basis for its clustering in caveolae.

10.1016/j.str.2021.04.006

Our current study employed single-particle cryoelectron microscopy to visualize multiple states of open and closed conformations of S protein at physiological pH 7.

Conformational flexibility and structural variability of SARS-CoV2 S protein

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10.1128/mBio.03690-20

Here, we report six structures of the trimeric AdeB multidrug efflux pump in the presence of ethidium bromide using single-particle cryoelectron microscopy (cryo-EM).

Cryoelectron Microscopy Structures of AdeB Illuminate Mechanisms of Simultaneous Binding and Exporting of Substrates

10.1017/S1431927621004177

Using structural techniques, including single-particle cryoelectron microscopy and X-ray crystallography, the laboratory has solved spike trimer-antibody structures that allow classifying antibodies with respect to spike recognition and neutralization.

Neutralizing antibodies against coronaviruses

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Single Particle Cryoelectron - Using single-particle cryoelectron microscopy (cryo-EM) and biochemical assays, we demonstrate that SAMase performs its function by not only degrading SAM but also by interacting with and efficiently inhibiting the host’s methionine S-adenosyltransferase (MAT), the enzyme that produces SAM. [1] Here, we reconstitute the mouse Ptc1 into lipid nanodiscs and determine its structure using single-particle cryoelectron microscopy. [2] Our current study employed single-particle cryoelectron microscopy to visualize multiple states of open and closed conformations of S protein at physiological pH 7. [3] Here, we report six structures of the trimeric AdeB multidrug efflux pump in the presence of ethidium bromide using single-particle cryoelectron microscopy (cryo-EM). [4] Using structural techniques, including single-particle cryoelectron microscopy and X-ray crystallography, the laboratory has solved spike trimer-antibody structures that allow classifying antibodies with respect to spike recognition and neutralization. [5]