Crystallization and preliminary X-ray crystallographic analysis of the ArsM arsenic(III) S - Adenosylmethionine methyltransferase

Kavitha Marapakala, A. Abdul Ajees, Jie Qin, Banumathi Sankaran, Barry P. Rosen

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

Arsenic is the most ubiquitous environmental toxin and carcinogen and consequently ranks first on the Environmental Protection Agencys Superfund Priority List of Hazardous Substances. It is introduced primarily from geochemical sources and is acted on biologically, creating an arsenic biogeocycle. A common biotransformation is methylation to monomethylated, dimethylated and trimethylated species. Methylation is catalyzed by the ArsM (or AS3MT) arsenic(III) S-adenosylmethionine methyltransferase, an enzyme (EC 2.1.1.137) that is found in members of every kingdom from bacteria to humans. ArsM from the thermophilic alga Cyanidioschyzon sp. 5508 was expressed, purified and crystallized. Crystals were obtained by the hanging-drop vapor-diffusion method. The crystals belonged to the monoclinic space group C2, with unit-cell parameters a = 84.85, b = 46.89, c = 100.35 Å, Β = 114.25° and one molecule in the asymmetric unit. Diffraction data were collected at the Advanced Light Source and were processed to a resolution of 1.76 Å.

Original languageEnglish
Pages (from-to)1050-1052
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume66
Issue number9
DOIs
Publication statusPublished - 01-09-2010

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

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