Crystallization and Preliminary Diffraction Studies of Malate Dehydrogenase from Streptomyces aureofaciens

Authors: Mikulasova, Darina; Tomaskova, Natasa; Maderova, Jana; Kollarova, Marta

Source: Protein and Peptide Letters, Volume 13, Number 2, February 2006 , pp. 207-210(4)

Publisher: Bentham Science Publishers

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Abstract:

Purified malate dehydrogenase (MDH) of Streptomyces aureofaciens was crystallized either in the absence or in the presence of NADH or NADPH coenzymes by hanging-drop vapour-diffusion method. An X-ray study has shown, that MDH crystals belong to space group C2221 with unit-cell parameters A = 53.2 Å, b = 104.6 Å, c = 520.0 Å, α = β = γ = 90° , MDH-NADH crystals to space group C2 with unit-cell parameters A = 51.5 Å, b = 51.5 Å, c = 256 Å, α = β = γ = 90 , and MDH-NADPH crystals to space group C2221 with unit-cell parameters A = 72, Å b = 72 Å, c = 520 Å, α = β = γ = 90° . The crystal of native MDH diffracted to 2.1 Å resolution.

Keywords: Malate dehydrogenase (MDH); Streptomyces aureofaciens; protein crystallization

Document Type: Research article

DOI: http://dx.doi.org/10.2174/092986606775101634

Affiliations: 1: Department of Biochemistry, Faculty of Natural Sciences, Comenius University, Mlynska dolina CH-1, 842 15 Bratislava, Slovak Republic.

Publication date: 2006-02-01

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Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.