論文

査読有り
2006年

Overexpression, purification, crystallization and preliminary X-ray cystallographic studies of a proline-specific aminopeptidase from Aneurinibacillus sp. strain AM-1

Acta Crystallographica Section F: Structural Biology and Crystallization Communications
  • Akioka, M.
  • ,
  • Nakano, H.
  • ,
  • Horikiri, A.
  • ,
  • Tsujimoto, Y.
  • ,
  • Matsui, H.
  • ,
  • Shimizu, T.
  • ,
  • Nakatsu, T.
  • ,
  • Kato, H.
  • ,
  • Watanabe, K.

62
12
開始ページ
1266
終了ページ
1268
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1107/S1744309106047543
出版者・発行元
BLACKWELL PUBLISHING

To elucidate the structure and molecular mechanism of a characteristic proline-specific aminopeptidase produced by the thermophile Aneurinibacillus sp. strain AM-1, its gene was cloned and the recombinant protein was overexpressed in Escherichia coli, purified and crystallized using the hanging-drop vapour-diffusion method. X-ray diffraction data were collected to 1.8 angstrom resolution from the recombinant aminopeptidase crystal. The crystals belong to the orthorhombic space group P2(1)2(1)2, with unit-cell parameters a = 93.62, b = 68.20, c = 76.84 angstrom. A complete data set was also obtained from crystals of SeMet-substituted aminopeptidase. Data in the resolution range 20-2.1 angstrom from the MAD data set from the SeMet-substituted crystal were used for phase determination.

リンク情報
DOI
https://doi.org/10.1107/S1744309106047543
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/17142913
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000242429700024&DestApp=WOS_CPL
URL
http://www.scopus.com/inward/record.url?eid=2-s2.0-33845484892&partnerID=MN8TOARS
ID情報
  • DOI : 10.1107/S1744309106047543
  • ISSN : 1744-3091
  • ORCIDのPut Code : 58433933
  • PubMed ID : 17142913
  • SCOPUS ID : 33845484892
  • Web of Science ID : WOS:000242429700024

エクスポート
BibTeX RIS