J
J. Bernard Heymann
Researcher at National Institutes of Health
Publications - 83
Citations - 5800
J. Bernard Heymann is an academic researcher from National Institutes of Health. The author has contributed to research in topics: Capsid & Image processing. The author has an hindex of 35, co-authored 79 publications receiving 5226 citations. Previous affiliations of J. Bernard Heymann include University of Basel & Albert Einstein College of Medicine.
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Journal ArticleDOI
Three-Dimensional Structure of Herpes Simplex Virus from Cryo-Electron Tomography
Kay Grünewald,Prashant Desai,Dennis C. Winkler,J. Bernard Heymann,J. Bernard Heymann,David M. Belnap,Wolfgang Baumeister,Alasdair C. Steven +7 more
TL;DR: Herpes simplex virus, a DNA virus of high complexity, consists of a nucleocapsid surrounded by the tegument—a protein compartment—and the envelope, which was seen to form an asymmetric cap in cryo–electron tomograms of isolated virions.
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Bsoft: image processing and molecular modeling for electron microscopy.
TL;DR: Bsoft is a software package written for image processing of electron micrographs, interpretation of reconstructions, molecular modeling, and general image processing that allows shell scripting of processes and allows subtasks to be distributed across multiple computers for concurrent processing.
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Influenza virus pleiomorphy characterized by cryoelectron tomography.
Audray K. Harris,Giovanni Cardone,Dennis C. Winkler,J. Bernard Heymann,Matthew Brecher,Judith M. White,Alasdair C. Steven +6 more
TL;DR: Cryoelectron tomography is used to visualize the 3D structures of 110 individual virions of the X-31 (H3N2) strain of influenza A, and some virions have substantial gaps in their matrix layer, and others appear to lack a matrix layer entirely, suggesting the existence of an alternative budding pathway in which matrix protein is minimally involved.
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The three-dimensional structure of aquaporin-1
Thomas Walz,Thomas Walz,Teruhisa Hirai,Kazuyoshi Murata,J. Bernard Heymann,Kaoru Mitsuoka,Yoshinori Fujiyoshi,Barbara L. Smith,Peter Agre,Andreas Engel +9 more
TL;DR: A model that identifies the aqueous pore in the AQP1 molecule and indicates the organization of the tetrameric complex in the membrane is provided.
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One number does not fit all: Mapping local variations in resolution in cryo-EM reconstructions
TL;DR: A space-frequency representation, the short-space Fourier transform, is proposed, to assess the quality of a density map, voxel-by-voxel, i.e. by local resolution mapping, to improve the interpretability of reconstructions.