July, 2017: Scientist Hugo Hilton from Prof. Parham's Lab joins Calico labs as Research Specialist  . .http://www.calicolabs.com/


July, 2017: Dave Bushnell- Senior Scientist at Kornberg Lab is getting e a promotion at SLAC-- as a Director of Cryo-EM operation for the SU/SLAC Cryo-EM center starting August 2017.

Dave Bushnell also will promote to a Chairman of the SSRL UEC starting October 2017.

Dave Bushnell is a Sr. Research Associate in the Department of Structural Biology at Stanford University.  His research focuses on using structural methods such as electron microscopy and protein crystallography to understand and control the process of gene expression.   Dave received his BS degree from Cornell University and went on to complete a PhD in Biophysics from Stanford University.   While working in the lab of Prof. Roger Kornberg, Dave was part of the team that solved the atomic structure of the 10-subunit yeast RNA Polymerase II which contributed to Prof. Kornberg being awarded the 2006 Nobel Prize in Chemistry.  Dave has continued his structural studies of RNA polymerase II mechanism including solving the structure of RNA Polymerase II with the inhibitor alpha-amanitin.  Recently he has been involved with Cocrystal Pharma Inc., a small start up that uses structure guided drug discovery techniques to develop novel anti-viral therapies.  Dave’s first beamtime at SSRL was May 5th, 1994 and he has been an active user ever since.  In addition to experience at SSRL he has performed experiments at LCLS, ALS, APS, CHESS and NSLS.  

July, 2017: Prof. Georgios Skiniotis joint the Department of Structural Biloligy.

Georgios Skiniotis is a structural biologist with expertise in electron cryo-microscopy (cryoEM).  Dr. Skiniotis has exploited the power of cryoEM to study a wide range of important biological “machines” or macromolecular assemblies.  His main interests are on the mechanisms of transmembrane signal instigation with a particular focus on G protein-coupled receptors and cytokine receptors.  The application of cryoEM to such systems has also driven him to explore and refine approaches for resolving technically challenging problems.

July, 2017: Scientist Hugo Hilton from Prof. Parham's Lab, joins Calico labs as Research Specialist  . .http://www.calicolabs.com/

July, 2017: Scientist Emily Wroblewski from Prof. Parham's Lab - Structural Biology Department, will join as a faculty at the Washington University-Saint Louis in September 2017.

  • October 9, 2013: Michael Levitt, PhD, wins the Nobel Prize in Chemistry
  • January 4, 2010: Xuhui Huang has accepted appointment as an Assistant Professor at the Department of Chemistry, The Hong Kong University of Science and Technology after working as a postdoc in Michael Levitt's lab. Congratulations on your achievment.
  • January 4, 2010: Dong Wang has accepted appointment as an Assistant Professor at the University of California San Diego after working as a postdoc in Roger Kornberg's lab. Our best wishes for continued success.
  • November 1, 2009: Craig Kaplan takes a faculty position with the Department of Biochemistry at Texas A&M. Craig was a postdoc in Roger Kornberg's lab. Congratulations and best of luck.
  • May, 2009: Elisabetta Viani Puglisi named Assistant Professor of Structural Biology.
  • February 11, 2008:  Ted Jardetzky elected a Fellow of the American Academy of Microbiology.
  • October 4, 2006: Roger Kornberg wins The Nobel Prize in Chemistry 2006
  • April 30, 2002:  Michael Levitt elected Member of the National Academy of Sciences.
    NAS Section: Biophysics and Computational Biology.
    Citation: Levitt is a biophysicist, who was one of the founders of modern computational biology. He has been a leader in developing important computational methods that allow us to analyze nucleic acid and protein structures, and he has been a pioneer in the theoretical investigations of the protein-folding problem.
  • November 1, 2001: Scholars Recognized by the American Association
    David B. McKay, Professor of Structural Biology, was cited "for crystallographic and biophysical studies providing insights in macromolecular structure and mechanisms of microbial virulence factors, molecular chaperone proteins, and catalytic RNAs."
    [Complete Article form the November 1, 2001 issue of "The Stanford Report"]
  • September 5, 2001: Researchers crack 'code' of elusive molecule that helps regulate fluid volume By Krista Conger
    Solving the three-dimensional structure of proteins is a bit like cracking the Mayan code: difficult yet rewarding. Each solution contributes to an overall understanding of how a cell functions. Now a Stanford University Medical Center laboratory has solved the structure of an important family of cellular receptors that eluded scientists for years.
    [Complete Article form the September 5, 2001 issue of "The Stanford Report"]
  • June 8, 2001: STRUCTURAL BIOLOGY: A Marvellous Machine for Making Messages By Aaron Klug
    The wonderful x-ray structures of RNA polymerase published in the past 3 years have revealed a wealth of information about how genes are transcribed. In an eloquent Perspective, Klug describes the latest tour de force from Kornberg's laboratory: the crystal structure of yeast RNA polymerase II in action.
    [Complete Article form the June 8, 2001 issue of "Science"]
  • May 23, 2001: Roger Kornberg has been awarded the 2001 Welch Award
    The creation of human life begins with a single cell that divides into two. But how does DNA tell each subsequent cell to become a blood cell, bone cell, tissue cell or some other specialized type? And why does this process sometimes malfunction, leading to birth defects, cancers and other diseases?

    Thanks in large part to the pioneering work of Stanford University's Roger D. Kornberg, scientists now are beginning to understand the process of copying DNA into RNA, called transcription. This knowledge ultimately will allow scientists to more effectively apply the results of the human genome project to better understand disease. Today, The Welch Foundation announced that Dr. Kornberg will receive its 2001 Welch Award, a $300,000 prize given for lifetime achievements in basic chemical research, in recognition of these contributions.
  • May 15, 2001: Michael Levitt has been elected a Fellow of the Royal Society.
    Professor Michael Levitt Professor and Chair, Computational Structural Biology, Department of Structural Biology, Stanford University School of Medicine, USA. Michael Levitt is distinguished for his highly original work in structural molecular biology, which focuses on protein folding and the computational analysis of structures. He discovered the four classes of protein folds, introduced automated secondary structure identification, and explained how the structural segments pack.