Journal
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
Volume 61, Issue -, Pages 288-290Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S174430910500299X
Keywords
-
Ask authors/readers for more resources
Alginate lyases depolymerize alginate, a heteropolysaccharide consisting of alpha-L-guluronate and beta-D-mannuronate, throuhg a beta-elimination reaction. the alginate lyases A1-II (25 kDa) and A1-II' (25kDa) from Sphingomonas sp. A1, primary structure but have different substrate specificities. To determine clearly the structural basis for substrate recognition in the depolymerization mechanism by alginate lyases, both proteins were crystallized at 293 K using the vapour-diffusion method. A crystal of A1-II belonged to space group P2(1) and diffracted to 2.2 angstrom resolution, with unit-cell parameters a = 51.3, b = 30.1, c = 101.6 angstrom, beta = 100.2 degrees, while a crystal of A1-II' belonged to space group P2(1)2(1)2(1) and diffracted to 1.0 angstrom resolution, with unit-cell parameters a= 34.6, b = 68.5, c = 80.3 angstrom.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available