Thomas Walz

  • Latest publications

    Hite RK, Chiu PL, Schuller JM, Walz T (2015) Effect of lipid head groups on double-layered two-dimensional crystals formed by aquaporin-0. PLoS One 10: e0117371.

    Blok NB, Tan D, Wang RY, Penczek PA, Baker D, DiMaio F, Rapoport TA, Walz T (2015) Unique double-ring structure of the peroxisomal Pex1/Pex6 ATPase complex revealed by cryo-electron microscopy. Proc Natl Acad Sci USA 112: E4017-4025.

    Chiu PL, Bou-Assaf GM, Chhabra ES, Chambers MG, Peters RT, Kulman JD, Walz T (2015) Mapping the interaction between factor VIII and von Willebrand factor by electron microscopy and mass spectrometry. Blood 126: 935-938.

    Hite RK, Yuan P, Li Z, Hsuing Y, Walz T, MacKinnon R (2015) Cryo-electron microscopy structure of the Slo2.2 Na+-activated K+ channel. Nature 527: 198-203.

    Tan D, Cai Y, Wang J, Zhang J, Menon S, Chou HT, Ferro-Novick S, Reinisch KM, Walz T (2013) The EM structure of the TRAPPIII complex leads to the identification of a requirement for COPII vesicles on the macroautophagy pathway. Proc Natl Acad Sci USA 110: 19432-19437.

  • Prizes and Awards

    Armenise-Harvard Junior Faculty Grant, Department of Integrative Biology & Physiology: “Electron Microscopy of Spliceosomes”, 2002

    Award for Outstanding Achievement in Biomedical Sciences (Sponsored by Genzyme)

Who he is

Tom Walz did his Ph.D. studies in Andreas Engel’s group at the University of Basel and his postdoctoral studies in Per Bullough’s group at the University of Sheffield, where he became a BBSRC David Phillips Research Fellow.

In 1999, Walz became an Assistant Professor in the Department of Cell Biology at Harvard Medical School and was promoted to Full Professor in 2007. From 1998 to 2015, he was an investigator with the Howard Hughes Medical Institute, and in 2015 he moved to the Rockefeller University, where he heads the Laboratory of Molecular Electron Microscopy.

What he does

The Walz group uses electron crystallography to determine the structure of membrane proteins, in particular aquaporins and transporters, and single-particle electron microscopy (EM) to visualize macromolecular complexes, currently focusing on complexes that play roles in vesicular transport, such as multisubunit tethering complexes.

A major focus of the group concerns the study of the structural basis that allows membrane proteins to perform their varied functions, taking advantage of the unique possibilities provided by EM. For example, membrane transporters are reconstituted into tubular crystals and exposed to different conditions to visualize the conformational changes that underlie substrate transport.

In parallel, a new approach is being established, based on single-particle cryo-EM of membrane proteins reconstituted into nanodiscs, to visualize how lipids regulate the conformation, and thus the function, of membrane proteins. Finally, the group engages in collaborations to help colleagues interested in using single-particle EM to answer their biological questions.

News from the Lab

The Walz group has recently initiated single-particle cryo-EM work on AAA ATPases, chromatin remodeling complexes as well as complexes associated with vesicular transport, in particular the BBSome and retromer complexes.