Structure determination of tubular crystals of membrane proteins. III. Solvent flattening

Koji Yonekura, Chikashi Toyoshima

Research output: Contribution to journalArticlepeer-review

17 Citations (Scopus)

Abstract

Solvent flattening is considered to be a principal means for improving the data quality in X-ray crystallography. It could be equally effective for tubular crystals of membrane proteins imaged by electron microscopy because of the large empty space inside the tubes. However, tubular crystals are difficult objects for solvent flattening due to lack of electron diffraction amplitudes. Therefore, solvent flattening was used to align images more accurately and to improve the completeness of the data by reducing contributions of noise in the solvent (+ lipid) region. The methods developed were tested with the tubular crystals of Ca2+-ATPase embedded in amorphous ice. The improvement of the data quality was remarkable when solvent flattening was applied to many individual images before averaging. In this way, noises contaminated in the protein region by contrast transfer function were removed effectively. Solvent flattening was far more powerful than simple averaging described in Part II of this series (K. Yonekura, C. Toyoshima, Ultramicroscopy 84 (2000) 15. Copyright (C) 2000 Elsevier Science B.V.

Original languageEnglish
Pages (from-to)29-45
Number of pages17
JournalUltramicroscopy
Volume84
Issue number1-2
DOIs
Publication statusPublished - 2000 Jul
Externally publishedYes

Keywords

  • Ca-ATPase
  • Cryo-electron microscopy
  • Solvent flattening
  • Tubular crystal

ASJC Scopus subject areas

  • Electronic, Optical and Magnetic Materials
  • Atomic and Molecular Physics, and Optics
  • Instrumentation

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