Crystallization of peptidase T from Salmonella typhimurium.
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 A, but a selenomethionine derivative of this protein did not yield good crystals. Crystals of the His-tag peptidase T diffracted to 2.6 A, 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.
Department of Microbiology, University of Illinois at Urbana-Champaign, B103 Chemical and Life Sciences Laboratory, Urbana, Illinois 61801, USA.
K
K
Håkansson
D
D
Broder
A H
AH
Wang
C G
CG
Miller
D000626:Aminopeptidases / Q000737:chemistry*; D001483:Base Sequence; D003460:Crystallization; D017931:DNA Primers; D011487:Protein Conformation; D012486:Salmonella typhimurium / Q000201:enzymology*
D017931:DNA Primers; D000626:Aminopeptidases; C039576:peptidase T