Crystallization and preliminary X-ray diffraction studies of tetrameric malate dehydrogenase from the novel Antarctic psychrophile Flavobacterium frigidimaris KUC-1

A psychrophilic malate dehydrogenase from the novel Antarctic bacterium F. frigidimaris KUC-1 was crystallized using the hanging-drop vapour-diffusion method. The crystals contained one tetrameric molecule per asymmetric unit. The best crystal diffracted to 1.8 Å resolution.

Bibliographic Details
Published in:Acta Crystallographica Section F Structural Biology and Crystallization Communications
Main Authors: Fujii, Tomomi, Oikawa, Tadao, Muraoka, Ikuo, Soda, Kenji, Hata, Yasuo
Format: Text
Language:English
Published: International Union of Crystallography 2007
Subjects:
Crystallization Communications
Antarctic
Antarc*
Online Access:http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2339744
http://www.ncbi.nlm.nih.gov/pubmed/18007057
https://doi.org/10.1107/S1744309107051524
Description
Summary:A psychrophilic malate dehydrogenase from the novel Antarctic bacterium F. frigidimaris KUC-1 was crystallized using the hanging-drop vapour-diffusion method. The crystals contained one tetrameric molecule per asymmetric unit. The best crystal diffracted to 1.8 Å resolution.

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