Year: 1999
Type: article
Abstract: Human mitochondrial NAD(P)(+)-dependent malic enzyme was overexpressed in Escherichia coli and purified by anion-exchange, ATP affinity, and gel filtration chromatography. The protein was crystallized with the hanging-drop vapor diffusion method. Many different crystal forms were observed, five of which were characterized in some detail. A 2.5-A multiple-wavelength anomalous diffraction data set and a 2.1-A native data set were collected using synchrotron radiation on crystals containing selenomethionyl residues. These crystals belong to space group B2, with a = 204.4 A, b = 107.0 A, c = 59.2 A, and gamma = 101.9 degrees. Self-rotation functions demonstrated that the tetramer of this enzyme obeys 222 symmetry.
Source: Journal of Structural Biology
Language: English
Subfield: Materials Chemistry
Field: Materials Science
Domain: Physical Sciences
Open Access status: hybrid
Estimated APC paid: $4,350
OpenAlex ID: W1994551673