Electron crystallography as a technique to study the structure on membrane proteins in a lipidic environment.
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Membrane protein structures without crystals, by single particle electron cryomicroscopyCryo-EM structure of the ribosome–SecYE complex in the membrane environmentMutual adaptation of a membrane protein and its lipid bilayer during conformational changesStructure of RPE65 isomerase in a lipidic matrix reveals roles for phospholipids and iron in catalysis.Self-assembled lipid and membrane protein polyhedral nanoparticles.Membrane protein structure determination using cryo-electron tomography and 3D image averaging.Single-particle electron microscopy in the study of membrane protein structureRemoval of Vesicle Structures From Transmission Electron Microscope ImagesThe New York Consortium on Membrane Protein Structure (NYCOMPS): a high-throughput platform for structural genomics of integral membrane proteins.Biophysics of α-synuclein membrane interactions.A pipeline for comprehensive and automated processing of electron diffraction data in IPLT.Structure of the BK potassium channel in a lipid membrane from electron cryomicroscopy.The use of trehalose in the preparation of specimens for molecular electron microscopySelf-aligned wet-cell for hydrated microbiology observation in TEM.Specimen preparation for electron diffraction of thin crystals.Regulation of human EGF receptor by lipidsA helical processing pipeline for EM structure determination of membrane proteinsMolecular driving forces defining lipid positions around aquaporin-0.High-density reconstitution of functional water channels into vesicular and planar block copolymer membranes.Mechanically, magnetically, and "rotationally aligned" membrane proteins in phospholipid bilayers give equivalent angular constraints for NMR structure determination.Specificity of intramembrane protein-lipid interactions.Visualization of bionanostructures using transmission electron microscopical techniques.Applications of NMR to membrane proteins.Protein structure determination by electron diffraction using a single three-dimensional nanocrystal.Two-dimensional crystallization of intact F-ATP synthase isolated from bovine heart mitochondria.Two-dimensional crystallization of monomeric bovine cytochrome c oxidase with bound cytochrome c in reconstituted lipid membranesTwo-dimensional protein crystals for solar energy conversion.Electron cryomicroscopy as a powerful tool in biomedical research.Lipid-Protein Interactions Are Unique Fingerprints for Membrane Proteins.
P2860
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P2860
Electron crystallography as a technique to study the structure on membrane proteins in a lipidic environment.
description
2009 nî lūn-bûn
@nan
2009 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Electron crystallography as a ...... eins in a lipidic environment.
@ast
Electron crystallography as a ...... eins in a lipidic environment.
@en
type
label
Electron crystallography as a ...... eins in a lipidic environment.
@ast
Electron crystallography as a ...... eins in a lipidic environment.
@en
prefLabel
Electron crystallography as a ...... eins in a lipidic environment.
@ast
Electron crystallography as a ...... eins in a lipidic environment.
@en
P1476
Electron crystallography as a ...... eins in a lipidic environment.
@en
P2093
Thomas Walz
P304
P356
10.1146/ANNUREV.BIOPHYS.050708.133649
P577
2009-01-01T00:00:00Z