MISC

2004年11月

Crystallographic characterization of the N-terminal domain of PEX1

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
  • K Shiozawa
  • ,
  • N Maita
  • ,
  • K Tomii
  • ,
  • A Seto
  • ,
  • N Goda
  • ,
  • Y Akiyama
  • ,
  • T Shimizu
  • ,
  • M Shirakawa
  • ,
  • H Hiroaki

60
開始ページ
2098
終了ページ
2099
記述言語
英語
掲載種別
DOI
10.1107/S090744490402428X
出版者・発行元
WILEY-BLACKWELL

Peroxisomal enzymes are responsible for several primary metabolism pathways, including beta-oxidation and lipid biosynthesis. PEX1 and PEX6 are hexameric AAA-type ATPases and both are necessary for the import of more than 50 peroxisomal resident proteins from the cytosol into peroxisomes. In this study, PEX1 N-terminal domain crystals have been prepared. The crystals belong to space group P3(1) or P3(2), with unit-cell parameters a=b=63.5 Angstrom, c=33.5 Angstrom, and contain one protein molecule per crystallographic asymmetric unit. An intensity data set was collected to a resolution of 2.05 Angstrom.

Web of Science ® 被引用回数 : 2

リンク情報
DOI
https://doi.org/10.1107/S090744490402428X
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000224595200042&DestApp=WOS_CPL
ID情報
  • DOI : 10.1107/S090744490402428X
  • ISSN : 1399-0047
  • Web of Science ID : WOS:000224595200042

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