Original scientific paper

Methionine Adenosyltransferase Purified from Rat Liver

Isabel Pérez-Mato ; Department of Biochemistry, University of Cambridge, 80 Tennis Court Road, Cambridge CB2 1GA, UK
Dijana Matak-Vinković ; Department of Biochemistry, University of Cambridge, 80 Tennis Court Road, Cambridge CB2 1GA, UK
Mladen Vinković ; Department of Biochemistry, University of Cambridge, 80 Tennis Court Road, Cambridge CB2 1GA, UK
José M. Mato ; Division of Hepatology and Gene Therapy, Department of Medicine, University of Navarra, 31008 Pamplona, Spain

Abstract

Methionine adenosyltransferase (MAT III), also known as S-adeno-sylmethionine synthetase, was purified from rat liver and crystallized. X-ray diffraction data were collected using a microfocused synchrotron radiation. The crystallization conditions were extensively optimized but final crystal size was never larger than 303 pm3. Due to their small size crystals had no detectable diffraction on either rotating anode source or the Deresbury SRS beamline 9.6 (GB). Finally, four data sets were collected on Grenoble ESRF (France) undulator microfocus beamline ID13 to resolution of 3.2-3.6 Å. Crystals belong to the cubic space group F432 with cell dimension a = 246 Å. Attempts are under way to solve the structure by molecular replacement, using recombinant MAT I rat liver structure as a search model.

Keywords

methionine adenosyltransferase; enzyme; microcrystals; microdiffraction

Hrčak ID:

127500

URI

https://hrcak.srce.hr/127500

Publication date:

4.2.2002.

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