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Our research uses 3-D electron microscopy (EM) to study structure and function at the resolution of molecules and supramolecular assembly within cells. This aspect of EM includes techniques such as electron crystallography, electron tomography, helical and “single particle” 3-D image reconstruction. Since we specialize in EM, we also spend considerable effort in method development particularly as it pertains to electron tomography (ET). Present efforts at method development are aimed at algorithms to improve the molecular images that we can obtain by ET. We moved from an emphasis on electron crystallography of 2-D arrays to ET to improve our 3-D images obtained from fast frozen, active insect flight muscle (IFM). To study actively contracting IFM, we needed images of individual cross-bridges and that is something that cannot be obtained by any of the other 3DEM techniques. In order to improve signal-to-noise ratio in these 3-D images but still maintaining the ability to distinguish different structures within the muscle lattice, we adapted methods for classifying images that were developed for single particle 3-D reconstruction in order to identify and group self-similar 3-D structures for subsequent averaging. These methods are enabling us to for the first time study the conformations of tension generating cross-bridges in situ.
Our work on rigor IFM revealed at least two different cross-bridge conformations within 2-headed myosin cross-bridges, one of which has a lever arm angle near 90° suggestive of a tension generating conformation. Our reconstructions of rigor muscle also showed a mixture of single headed and double headed cross-bridges. Recently, by swelling the muscle fibers in rigor, we have been able for the first time to see and determine the amount of S2 that is free of the filament backbone and that the can modulate the ability of myosin heads to search for actin. We also found out that the origins of rigor cross-bridges are not as predicted by current models of myosin head action which are based on X-ray crystallography.
Our work on rigor IFM revealed at least two different cross-bridge conformations within 2-headed myosin cross-bridges, one of which has a lever arm angle near 90° suggestive of a tension generating conformation. Our reconstructions of rigor muscle also showed a mixture of single headed and double headed cross-bridges. Recently, by swelling the muscle fibers in rigor, we have been able for the first time to see and determine the amount of S2 that is free of the filament backbone and that the can modulate the ability of myosin heads to search for actin. We also found out that the origins of rigor cross-bridges are not as predicted by current models of myosin head action which are based on X-ray crystallography.
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PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICAno. 9 (2024): e2311883121-e2311883121
Hojjatian AH,Jun Liu, Taylor DWT, Daneshparvar ND, Winkler HW, Ye FY, Fagnant PMF,Kathleen M. Trybus,Kenneth A. Taylor
EMPIAR dataset (2023)
Microscopy and microanalysis : the official journal of Microscopy Society of America, Microbeam Analysis Society, Microscopical Society of Canadano. 29 Suppl 1 (2023): 912-914
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCESno. 19 (2023): 14936-14936
Microscopy and microanalysis : the official journal of Microscopy Society of America, Microbeam Analysis Society, Microscopical Society of Canadano. 29 Suppl 1 (2023): 917-919
Microscopy and microanalysis : the official journal of Microscopy Society of America, Microbeam Analysis Society, Microscopical Society of Canadano. Supplement_1 (2023): 958-959
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Journal of structural biologyno. 3 (2023): 107995-107995
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