Open AccessCrystallization and preliminary X‐ray analysis of alginate lyases A1‐II and A1‐II′ from Sphingomonas sp. A1
Author(s) -
Yamasaki Masayuki,
Ogura Kohei,
Moriwaki Satoko,
Hashimoto Wataru,
Murata Kousaku,
Mikami Bunzo
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430910500299x
Subject(s) - crystallization , x ray , materials science , crystallography , chemistry , physics , optics , organic chemistry
Alginate lyases depolymerize alginate, a heteropolysaccharide consisting of α‐ l ‐guluronate and β‐ d ‐mannuronate, through a β‐elimination reaction. The alginate lyases A1‐II (25 kDa) and A1‐II′ (25 kDa) from Sphingomonas sp. A1, which belong to polysaccharide lyase family PL‐7, exhibit 68% homology in 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 P 2 1 and diffracted to 2.2 Å resolution, with unit‐cell parameters a = 51.3, b = 30.1, c = 101.6 Å, β = 100.2°, while a crystal of A1‐II′ belonged to space group P 2 1 2 1 2 1 and diffracted to 1.0 Å resolution, with unit‐cell parameters a = 34.6, b = 68.5, c = 80.3 Å.