Jiusheng, Lin


Jiusheng Lin has a PhD from Lanzhou University, and received his primary structural biology training in Dr. Mark Wilson's Lab at UNL. He has over ten years’ research experience working in structural biology, protein science and biochemistry, having solved the molecular structures of many biological macromolecules using conventional and serial X-ray crystallography, neutron crystallography, and Cryo-EM. As a Senior Research Associate working in Department of Biochemistry, he is interested in understanding the biochemical and biophysical basis of protein function by using a combination of structural biological, biophysical, and biochemical approaches.

Current Projects:

Supervised by Dr. Jennifer Clarke and Dr. Mark Wilson, a few examples of ongoing projects include:

 1). Proton location in short hydrogen bonds: Short hydrogen bonds (donor-acceptor distances ≤ 2.5 Å) are thought to play key functional roles in proteins. The location of the proton in these short hydrogen bonds is important but difficult to determine experimentally. We are using a combination of x-ray and neutron crystallography, database mining, and statistical analysis to study short hydrogen bonds and to use the resulting biophysical knowledge to better understand the roles of these controversial hydrogen bonds in biochemistry.


2)  Uncovering the function of a new family of DNA-binding proteins: The Escherichia coli protein YaaA is a member of the DUF328 family that is protective against oxidative stress. We have recently shown that YaaA is a representative of a new class of DNA-binding proteins with a new protein fold family that we’ve named the cantaloupe fold (Prahlad et al., JBC 2020). We are combining structural biology, computational approaches, biochemistry, and microbiology to understand how this protein protects bacteria from oxidative stress.

3) Transient motions during enzyme catalysis: Enzyme motion is known to be functionally important, but it has been difficult to experimentally study non-equilibrium motions that occur during enzyme catalysis.  We are using time-resolved mix-and-inject serial crystallography at X-ray free electron laser (XFEL) and synchrotron sources to directly observe the transient, functionally important motions during catalysis.

4) Serve as a structural biology project consultant: I provide help to interested researchers at the University of Nebraska to develop structural biology workflows that conform to current best practices. This includes support for data collection strategies at home and national user facilities, assistance with data analysis, and data management and archiving.