title: Crystallization of mouse S-adenosyl-L-homocysteine hydrolase.
abstract: S-adenosyl-L-homocysteine hydrolase (SAHH; EC 3.3.1.1) catalyzes the reversible hydrolysis of S-adenosyl-L-homocysteine to adenosine and L-homocysteine. For crystallographic investigations, mouse SAHH (MmSAHH) was overexpressed in bacterial cells and crystallized using the hanging-drop vapour-diffusion method in the presence of the reaction product adenosine. X-ray diffraction data to 1.55 A resolution were collected from an orthorhombic crystal form belonging to space group I222 with unit-cell parameters a = 100.64, b = 104.44, c = 177.31 A. Structural analysis by molecular replacement is in progress.
authors.affiliation: School of Pharmacy, Showa University, Tokyo 142-8555, Japan.
authors.forename: Masaaki
authors.initials: M
authors.lastname: Ishihara
authors.forename: Yoshio
authors.initials: Y
authors.lastname: Kusakabe
authors.forename: Tsuyoshi
authors.initials: T
authors.lastname: Ohsumichi
authors.forename: Nobutada
authors.initials: N
authors.lastname: Tanaka
authors.forename: Masayuki
authors.initials: M
authors.lastname: Nakanishi
authors.forename: Yukio
authors.initials: Y
authors.lastname: Kitade
authors.forename: Kazuo T
authors.initials: KT
authors.lastname: Nakamura
mesh_terms: D043383:Adenosylhomocysteinase / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D000818:Animals; D018360:Crystallography, X-Ray; D015870:Gene Expression; D051379:Mice
chemical_list: D043383:Adenosylhomocysteinase