The Cryoelectron Microscopy Structure of the Type 1 Chaperone-Usher Pilus Rod.
Hospenthal MK +7 more
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Structure of the recombinant alphavirus Western equine encephalitis virus revealed by cryoelectron microscopy. [PDF]
Sherman MB, Weaver SC.
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Structural dependence of HET-s amyloid fibril infectivity assessed by cryoelectron microscopy. [PDF]
Mizuno N, Baxa U, Steven AC.
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Author Correction: Structural dynamics of the midnolin-proteasome during ubiquitin-independent substrate turnover. [PDF]
Zhu C +7 more
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Visualization of the interaction between sphingomyelin and cholesterol in lipid bilayer membranes. [PDF]
Smothers JC +5 more
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Ultrastructural insights into the polar tube invasion organelle from microsporidian parasites. [PDF]
Watson PR, Ekiert DC, Bhabha G.
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SUN5 forms a regular protein lattice reinforcing the sperm head-tail junction. [PDF]
Moecking J +3 more
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Structural characterization of the HDV virion and its ribonucleoprotein. [PDF]
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Cryoelectron microscopy of refrozen cryosections
Journal of Structural Biology, 2003Cryoelectron microscopy makes it possible to record high-resolution detail from large and complex structures. However, its application to understanding cellular structure is limited by the requirement that samples should be no thicker than approximately 0.5-1 microm.
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Cryoelectron microscopy and cryoelectron tomography of the nuclear pre-mRNA processing machine
Journal of Structural Biology, 2002Large nuclear ribonucleoprotein particles, which can be viewed as the naturally assembled precursor messenger RNA (pre-mRNA) processing machine, were analyzed in frozen-hydrated preparations by cryoelectron microscopy. A general and reproducible strategy for preparing ice-embedded large nuclear ribonucleoprotein (lnRNP) particles at sufficiently high ...
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