Crystallization and preliminary X‐ray diffraction analysis of the S‐adenosylhomocysteine hydrolase (SAHH) from Thermotoga maritima. Issue 11 (5th November 2014)

• Record Type: Journal Article
• Authors: He, Miao; Zheng, Yingying; Huang, Chun‐Hsiang; Qian, Guojun; Xiao, Xiansha; Ko, Tzu‐Ping; Shao, Weilan; Guo, Rey‐Ting
• Is Part Of: Acta crystallographica. Volume 70:Issue 11(2014:Nov.)
• Page Start: 1563
• Page End: 1565
• Publication Date: 2014-11-05
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X14013478
• Languages: English
• ISSNs: 2053-230X

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <italic>S</italic>‐Adenosylhomocysteine hydrolase (SAHH) catalyzes the reversible conversion of <italic>S</italic>‐adenosylhomocysteine into adenosine and homocysteine. The SAHH from <italic>Thermotoga maritima</italic> (<italic>Tm</italic>SAHH) was expressed in <italic>Escherichia coli</italic> and the recombinant protein was purified and crystallized. <italic>Tm</italic>SAHH crystals belonging to space group <italic>C</italic>2, with unit‐cell parameters <italic>a</italic> = 106.3, <italic>b</italic> = 112.0, <italic>c</italic> = 164.9 Å, β = 103.5°, were obtained by the sitting‐drop vapour‐diffusion method and diffracted to 2.85 Å resolution. Initial phase determination by molecular replacement clearly indicated that the crystal contains one homotetramer per asymmetric unit. Further refinement of the crystal structure is in progress.</p> </abstract>