About
Wah Chiu is the Wallenberg-Bienenstock Professor and Professor of Bioengineering and, by courtesy, of Microbiology and Immunology at Stanford University. He is a pioneer in methodology development for cryogenic electron microscopy (cryo-EM). His work has made multiple transformational contributions in developing single particle cryo-EM as a tool for the structural determination of molecular machines at atomic resolution. His lab has solved many cryo-EM structures including viruses, chaperonins, membrane proteins, ion channels, antigen-antibody complexes, protein-RNA complexes, and RNA in collaboration with many scientists around the world. He continues to establish high standard testing and characterization protocols for cryo-EM instrumentation and to develop new image processing and modeling algorithms for cryo-EM structure determination. His current research focuses on developing cryogenic electron tomography (cryo-ET) to determine near atomic resolution structures of molecular complexes in situ.
Research topics
- Computer Science
- Biology
- Computational biology
- Chemistry
- Nanotechnology
- Engineering
- Chemical engineering
- Embedded system
- Physics
- Biochemistry
- Materials science
- Data science
- Virology
- Composite material
- Genetics
- Cell biology
- Molecular biology
Selected publications
Capturing the swelling of solid-electrolyte interphase in lithium metal batteries
Science · 2022 · 430 citations
- Materials science
- Nanotechnology
- Chemical engineering
Although liquid-solid interfaces are foundational in broad areas of science, characterizing this delicate interface remains inherently difficult because of shortcomings in existing tools to access liquid and solid phases simultaneously at the nanoscale. This leads to substantial gaps in our understanding of the structure and chemistry of key interfaces in battery systems. We adopt and modify a thin film vitrification method to preserve the sensitive yet critical interfaces in batteries at native liquid electrolyte environments to enable cryo–electron microscopy and spectroscopy. We report substantial swelling of the solid-electrolyte interphase (SEI) on lithium metal anode in various electrolytes. The swelling behavior is dependent on electrolyte chemistry and is highly correlated to battery performance. Higher degrees of SEI swelling tend to exhibit poor electrochemical cycling.
Target highlights in <scp>CASP14</scp> : Analysis of models by structure providers
Proteins Structure Function and Bioinformatics · 2021 · 39 citations
- Computer Science
- Computer Science
- Computational biology
The biological and functional significance of selected Critical Assessment of Techniques for Protein Structure Prediction 14 (CASP14) targets are described by the authors of the structures. The authors highlight the most relevant features of the target proteins and discuss how well these features were reproduced in the respective submitted predictions. The overall ability to predict three-dimensional structures of proteins has improved remarkably in CASP14, and many difficult targets were modeled with impressive accuracy. For the first time in the history of CASP, the experimentalists not only highlighted that computational models can accurately reproduce the most critical structural features observed in their targets, but also envisaged that models could serve as a guidance for further studies of biologically-relevant properties of proteins.
Cryo-EM model validation recommendations based on outcomes of the 2019 EMDataResource challenge
Nature Methods · 2021 · 118 citations
Senior authorCorresponding- Computer Science
- Computational biology
- Computer Science
This paper describes outcomes of the 2019 Cryo-EM Model Challenge. The goals were to (1) assess the quality of models that can be produced from cryogenic electron microscopy (cryo-EM) maps using current modeling software, (2) evaluate reproducibility of modeling results from different software developers and users and (3) compare performance of current metrics used for model evaluation, particularly Fit-to-Map metrics, with focus on near-atomic resolution. Our findings demonstrate the relatively high accuracy and reproducibility of cryo-EM models derived by 13 participating teams from four benchmark maps, including three forming a resolution series (1.8 to 3.1 Å). The results permit specific recommendations to be made about validating near-atomic cryo-EM structures both in the context of individual experiments and structure data archives such as the Protein Data Bank. We recommend the adoption of multiple scoring parameters to provide full and objective annotation and assessment of the model, reflective of the observed cryo-EM map density.
Nature Communications · 2020 · 43 citations
- Virology
- Biology
- Cell biology
Members of the Herpesviridae, including the medically important alphaherpesvirus varicella-zoster virus (VZV), induce fusion of the virion envelope with cell membranes during entry, and between cells to form polykaryocytes in infected tissues. The conserved glycoproteins, gB, gH and gL, are the core functional proteins of the herpesvirus fusion complex. gB serves as the primary fusogen via its fusion loops, but functions for the remaining gB domains remain unexplained. As a pathway for biological discovery of domain function, our approach used structure-based analysis of the viral fusogen together with a neutralizing antibody. We report here a 2.8 Å cryogenic-electron microscopy structure of native gB recovered from VZV-infected cells, in complex with a human monoclonal antibody, 93k. This high-resolution structure guided targeted mutagenesis at the gB-93k interface, providing compelling evidence that a domain spatially distant from the gB fusion loops is critical for herpesvirus fusion, revealing a potential new target for antiviral therapies.
Measurement of atom resolvability in cryo-EM maps with Q-scores
Nature Methods · 2020 · 438 citations
Senior authorCorresponding- Computer Science
- Computer Science
- Computational biology
Recent grants
NIH · $15.7M · 2010
NIH · $12.5M · 2022
NIH · $1.2M · 1993
NIH · $15.1M · 2020
NIH · $430k · 2022
Frequent coauthors
- 287 shared
Michael F. Schmid
SLAC National Accelerator Laboratory
- 220 shared
Kaiming Zhang
University of Science and Technology of China
- 208 shared
Grigore Pintilie
Clark University
- 157 shared
Shanshan Li
Ocean University of China
- 111 shared
Steven J. Ludtke
Baylor College of Medicine
- 93 shared
Joanita Jakana
Baylor College of Medicine
- 89 shared
Zhaoming Su
Sichuan University
- 75 shared
Matthew L. Baker
The University of Texas Health Science Center at Houston
Education
- 1975
PhD, Biophysics
University of California Berkeley
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