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.
Published in: | Acta Crystallographica Section F Structural Biology and Crystallization Communications |
---|---|
Main Authors: | , , , , |
Format: | Text |
Language: | English |
Published: |
International Union of Crystallography
2007
|
Subjects: | |
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 |
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. |
---|