Single particle refinement in electron crystallography : A pilot study

• Electron crystallography can be used to determine the structures of membrane proteins at near-atomic resolution in some cases. However, most electron crystallography projects remain at a resolution around 10 Å. This might be partly due to lack of flatness of many two-dimensional crystals. We have investigated this problem and suggest single particle processing of locally averaged unit cells to improve the quality and possibly the resolution of three-dimensional maps. Applying this method to the secondary transporter melibiose permease we have calculated a three-dimensional map that is clearer and easier to interpret than the map derived using purely electron-crystallographic methods.

Ämnesord

NATURVETENSKAP  -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)

NATURAL SCIENCES  -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)

NATURVETENSKAP  -- Biologi (hsv//swe)

NATURAL SCIENCES  -- Biological Sciences (hsv//eng)

Nyckelord

Crystal distortion

Electron crystallography

Membrane proteins

Single particle reconstruction

melibiose

membrane protein

permease

article

calculation

crystal structure

crystallography

elementary particle

measurement

pilot study

priority journal

protein structure

structure analysis

three dimensional imaging

Computer Simulation

Crystallization

Escherichia coli Proteins

Fourier Analysis

Imaging

Three-Dimensional

Microscopy

Electron

Transmission

Models

Molecular

Pilot Projects

Protein Conformation

Symporters

Biology

Publikations- och innehållstyp

ref (ämneskategori)

art (ämneskategori)