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    The research in our laboratory combines the powers of X-ray crystallography and electron cryo-microscopy to understand, at the atomic or near atomic resolution, the structures and functions of macromolecular assemblies from viruses and pathogenic bacteria. Those viruses and bacteria cause a variety of human diseases ranging from pneumonia, meningitis and shigellosis to mucocutaneous lesions, encephalitis and several forms of cancer. We are particularly interested in DNA viruses such as bacteriophages, herpes simplex virus, Kaposi's sarcoma-associated herpesvirus and human parvovirus, and several RNA viruses. Bacteria under our research include Gram-negative bacteria such as Shigella flexneri and Gram-positive bacteria such as Bacillus subtilis and Staphylococcus aureus. We aim to elucidate the chemical and physical bases of the replication cycles and infections of those microbes by bridging atomic details to cellular and organismal phenomena. We've identified antiviral targets against human herpesviruses and helped develop small-molecule inhibitors that can lead to antivirals. Our research can open new avenues to better ways for treatment, cure and prevention of diseases caused by those viral and microbial pathogens.


 
 

We utilize X-ray crystallography to unveil intricate workings of biological systems at the atomic detail. Shown above is a montage of the molecular structure of virus DNA-packaging terminase in complex with beta-thujaplicinol (red), a natural product isolated from Western red cedar, which serves as an anti-herpesvirus candidate. The structure sheds lights on the detailed molecular mechanism that can only be seen at such an atomic resolution, and also shows how the compound binds to the terminase active site thus blocks its function.

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gp1

The bacterial virus Sf6 DNA-packaging nano-machine as an ring-like octameric molecular assembly


sf6inject

Bacterial virus Sf6 DNA-injection apparatus. Background is a cryoEM image collected with a direct electron detector


sf6

CryoEM structure of bacterial virus Sf6


sf6 capsid pseudoatomic model

A pseudoatomic model of the bacterial virus Sf6 capsid consisting of over 1.35 million non-hydrogen atoms and with an overall mass of over 23 million Dalton. An icosahedral asymmetric unit consisting of seven capsid protein subunits is shown as a ribbon diagram.


aa

Replication initiator protein NS1 N-terminal Ori-binding/nickase domain from human bocavirus, an emerging pathogen infecting children


aa

The molecular motor that resolves concatemeric DNA into genome-length units and packages them into procapsids in bacterial virus Sf6


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The terminase nuclease domain of human herpes simplex virus


gp2

Targeting herpesvirus terminase using a group of compounds based on a natural product isolated from Western red cedar


aa

Phosphorylation of response regulator YycF (molecular surface) by the cognate histidine protein kinase YycG (ribbon diagram), a common mechanism in Gram-positive pathogenic bacteria such as Staphylococcus aureus and Bacillus anthracis


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X-ray data collection at the Advanced Photon Source using the raster function for a very long, thin Sf6 gp2 crystal


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State-of-the-art X-ray data collection at the Advanced Photon Source using raster for a very long, thin Sf6 gp2 crystal

   

       Our works have been featured on covers of many journals due to general interest to the scientific community:

   
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