Crystallization of peptidase T from Salmonella typhimurium

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

Research output: Contribution to journalArticlepeer-review

9 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)924-926
Number of pages3
JournalActa Crystallographica Section D: Biological Crystallography
Issue number7
Publication statusPublished - 2000
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology


Dive into the research topics of 'Crystallization of peptidase T from Salmonella typhimurium'. Together they form a unique fingerprint.

Cite this