Two-dimensional Crystallization of Membrane Proteins

• Nishino Yuri

  Bio-multisome research team, RIKEN Harima institute

• Miyazawa Atsuo

  Bio-multisome research team, RIKEN Harima institute

Bibliographic Information

Other Title

• 膜タンパク質の二次元結晶化法
• マク タンパクシツ ノ 2ジゲン ケッショウカホウ

Abstract

Membrane proteins play crucial roles in the mechanism underlying several aspects of cellular function. Nowadays　there are so many attempts for structural studies of proteins, because we believe that the structures give us a lot of　information to understand the functions and mechanisms. Electron crystallography is a way of the structure analysis　by electron microscopy using two-dimensional crystals of the membrane proteins. It is also quite difficult to make the　two-dimensional crystals, as well as the three-dimensional crystals for X-ray crystallography. The number of the　structures solved by electron crystallography is much less than that solved by X-ray. However, it should be a great　advantage that the electron crystallography can analyze the structure of membrane proteins which exist in the lipid　bilayer as they were in vivo. In this manuscript, we would introduce the methods of two-dimensional crystallization　summarizing only a few successful attempts.

Journal

• MEMBRANE

  MEMBRANE 32 (1), 25-31, 2007

  THE MEMBRANE SOCIETY OF JAPAN

Keywords

• membrane protein
• two-dimensional crystallization
• electron crystallography

Details

• CRID: 1390282681398379776
• NII Article ID: 10018696255
• NII Book ID: AN0023215X
• DOI: 10.5360/membrane.32.25
• ISSN: 18846440
• ISSN: 03851036
• NDL BIB ID: 8662459
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I8662459
• Web Site: https://www.jstage.jst.go.jp/article/membrane/32/1/32_25/_pdf
• Web Site: https://search.jamas.or.jp/link/ui/2007135575
• Text Lang: ja
• Data Source:
  • JaLC
  • NDL
  • Crossref
  • CiNii Articles
  • KAKEN
• Abstract License Flag: Disallowed