NDLI: Crystallization of mouse S-adenosyl-L-homocysteine hydrolase.

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Crystallization of mouse S-adenosyl-L-homocysteine hydrolase.

Content Provider	Europe PMC
Author	Ishihara, Masaaki Kusakabe, Yoshio Ohsumichi, Tsuyoshi Tanaka, Nobutada Nakanishi, Masayuki Kitade, Yukio Nakamura, Kazuo T.
Copyright Year	2010
Description	Mouse S-adenosyl-l-homocysteine hydrolase has been crystallized in the presence of the reaction product adenosine. Diffraction data to 1.55 Å resolution were collected using synchrotron radiation. 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 Å 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 Å. Structural analysis by molecular replacement is in progress.
Related Links	https://europepmc.org/backend/ptpmcrender.fcgi?accid=PMC2833045&blobtype=pdf
Volume Number	66
PubMed Central reference number	PMC2833045
Issue Number	Pt 3
Issue Number	pt 3
PubMed reference number	20208169
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications [Acta Crystallogr Sect F Struct Biol Cryst Commun]
e-ISSN	17443091
DOI	10.1107/s1744309110000771
Language	English
Publisher	International Union of Crystallography
Publisher Date	2010-02-24
Access Restriction	Open
Rights License	© International Union of Crystallography 2010
Subject Keyword	S-adenosyl-l-homocysteine hydrolase SAHH
Content Type	Text
Resource Type	Article
Subject	Biochemistry Condensed Matter Physics Genetics Biophysics Structural Biology

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