Shilton_1996_Protein.Sci_5_395

Reference

Title : Crystallization of a soluble form of the Kex1p serine carboxypeptidase from Saccharomyces cerevisiae - Shilton_1996_Protein.Sci_5_395
Author(s) : Shilton BH , Li Y , Tessier D , Thomas DY , Cygler M
Ref : Protein Science , 5 :395 , 1996
Abstract :

A soluble form of the killer factor and prohormone-processing carboxypeptidase, "Kex1 delta p," from Saccharomyces cerevisiae, has been crystallized in 17-22% poly(enthylene glycol) methyl ether (average M(r) = 5,000), 100 mM ammonium acetate, 5% glycerol, pH 6.5, at 20 degrees C. A native data set (2.8 A resolution) and four derivative data sets (3.0-3.2 A resolution) were collected at the Photon Factory (lambda = 1.0 A). The crystals belong to space group P2(1)2(1)2(1) with a =56.6 A, b = 84.0 A, c = 111.8 A. Freezing a Kex1 delta p crystal has facilitated the collection of a 2.4-A data set using a rotating anode source (lambda = 1.5418 A). Molecular replacement models have been built based on the structures of wheat serine carboxypeptidase (CPDW-II; Liao DI et al., 1992, Biochemistry 31:9796-9812) and yeast carboxypeptidase Y.

PubMedSearch : Shilton_1996_Protein.Sci_5_395
PubMedID: 8745419
Gene_locus related to this paper: yeast-kex01

Related information

Gene_locus yeast-kex01
Family yeast-kex01    Carboxypeptidase_S10
Structure yeast-kex01    Carboxypeptidase_S10    1AC5

Citations formats

Shilton BH, Li Y, Tessier D, Thomas DY, Cygler M (1996)
Crystallization of a soluble form of the Kex1p serine carboxypeptidase from Saccharomyces cerevisiae
Protein Science 5 :395

Shilton BH, Li Y, Tessier D, Thomas DY, Cygler M (1996)
Protein Science 5 :395