Crystallization of peptidase T from Salmonella typhimurium

Kjell Håkansson, Dan Broder, Andrew H.J. Wang, Charles G. Miller

研究成果: 雜誌貢獻文章同行評審

9 引文 斯高帕斯(Scopus)

摘要

Aminotripeptidase (peptidase T) from Salmonella typhimurium and a derivative carrying a C-terminal His tag have been crystallized. In both cases, the space group was found to be C2, with a single molecule in the asymmetric unit. Crystals of the native peptidase T diffract to 2.9 Å, but a selenomethionine derivative of this protein did not yield good crystals. Crystals of the His-tag peptidase T diffracted to 2.6 Å, however, and could be used for the production of good-quality selenomethionine crystals. All 15 methionines, a native metal ion and two mercury reactive sites could be located and crystals suitable for MAD data collection have been produced.

原文英語
頁(從 - 到)924-926
頁數3
期刊Acta Crystallographica Section D: Biological Crystallography
56
發行號7
DOIs
出版狀態已發佈 - 2000
對外發佈

ASJC Scopus subject areas

  • 結構生物學

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