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International Union of Crystallography, Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 9(63), p. 751-753, 2007

DOI: 10.1107/s1744309107036263

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Purification, crystallization and preliminary X-ray analysis of the galacto-N-biose-/lacto-N-biose I-binding protein (GL-BP) of the ABC transporter fromBifidobacterium longumJCM1217

Journal article published in 2007 by Jun Wada, Ryuichiro Suzuki, Shinya Fushinobu, Motomitsu Kitaoka, Takayoshi Wakagi, Hirofumi Shoun, Hisashi Ashida, Hidehiko Kumagai, Takane Katayama ORCID, Kenji Yamamoto
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This paper is available in a repository.

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Abstract

A recombinant galacto-N-biose-/lacto-N-biose I-binding protein (GL-BP) from Bifidobacterium longum JCM1217 has been prepared and crystallized by the hanging-drop vapour-diffusion method using 10 mg ml(-1) purified enzyme, 0.01 M zinc sulfate, 0.1 M MES buffer pH 5.9-6.4 and 20-22%(v/v) PEG MME 550 in the presence of 5 mM disaccharide ligands. Suitable crystals grew after 10 d incubation at 293 K. The crystals belong to space group C222(1), with unit-cell parameters a = 106.3, b = 143.6, c = 114.6 A for the lacto-N-biose I complex and a = 106.4, b = 143.4, c = 115.5 A for the galacto-N-biose complex, and diffracted to 1.85 and 1.99 A resolution, respectively.