| Autor: |
Bhargava, Girija, Mui, Suet, Pav, Susan, Wu, Hao, Loeber, Gerhard, Tong, Liang |
| Zdroj: |
Journal of Structural Biology; August 1999, Vol. 127 Issue: 1 p72-75, 4p |
| Abstrakt: |
Human mitochondrial NAD(P)+-dependent malic enzyme was overexpressed in Escherichia coliand 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-Å multiple-wavelength anomalous diffraction data set and a 2.1-Å native data set were collected using synchrotron radiation on crystals containing selenomethionyl residues. These crystals belong to space group B2, with a= 204.4 Å, b= 107.0 Å, c= 59.2 Å, and γ = 101.9°. Self-rotation functions demonstrated that the tetramer of this enzyme obeys 222 symmetry. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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