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Christopher Buser

Researcher at University of California, Berkeley

Publications -  25
Citations -  809

Christopher Buser is an academic researcher from University of California, Berkeley. The author has contributed to research in topics: Mutant & Neurotransmission. The author has an hindex of 13, co-authored 21 publications receiving 678 citations. Previous affiliations of Christopher Buser include University of Ulm.

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Journal ArticleDOI

Freeze-substitution: the addition of water to polar solvents enhances the retention of structure and acts at temperatures around -60 degrees C.

TL;DR: It is found that the visibility of structural details was optimal with acetone and that extraction increased with both increasing and decreasing solvent polarity, and the addition of water to polar solvents increased the sample quality, while being destructive when added to apolarsolvents.
Book ChapterDOI

"Tips and tricks" for high-pressure freezing of model systems

TL;DR: This chapter discusses some of the "little" things that can make the difference between successful or unsuccessful freezing, and covers all aspects of HPF, from specimen loading to removing your sample from the carriers in polymerized resin.
Journal ArticleDOI

Determinants of endocytic membrane geometry, stability, and scission

TL;DR: The results reveal that dynamic interplay between a lipid phosphatase, actin assembly, and membrane-sculpting proteins leads to proper membrane shaping, tubule stabilization, and scission in yeast.
Journal ArticleDOI

Cytomegalovirus Primary Envelopment Occurs at Large Infoldings of the Inner Nuclear Membrane

TL;DR: Large tubular infoldings of the inner nuclear membrane that were free of lamina and active in primary envelopment and subsequent transport of capsids to the nuclear periphery demonstrated that this structure represents a virus-induced specialized membrane domain at which the particles are preferentially enveloped.
Journal ArticleDOI

Major Tegument Protein pp65 of Human Cytomegalovirus Is Required for the Incorporation of pUL69 and pUL97 into the Virus Particle and for Viral Growth in Macrophages

TL;DR: It is concluded that pp65 is required for the incorporation of other viral proteins into the virus particle and thus is involved in the protein-protein interaction network leading to normal tegument formation.