| Autor: |
Baker, Heather M., Brown, Rosemary L., Dobbs, Aaron J., Blackwell, Leonard F., Buckley, Paul D., Hardman, Michael J., Hill, Jeremy P., Kitson, Kathryn E., Kitson, Trevor M., Baker, Edward N. |
| Zdroj: |
JMB Online (Journal of Molecular Biology); August 1994, Vol. 241 Issue: 2 p263-264, 2p |
| Abstrakt: |
The cytosolic (Class 1) aldehyde dehydrogenase (AIDH) from sheep liver has been crystallized in a form suitable for X-ray diffraction studies. The crystals, grown by vapour diffusion using 6·5 to 7·5% methoxypolyethylene glycol 5000 as precipitant, at pH 6·5, are orthorhombic with cell dimensions a= 80·7, b= 92·5, c= 151·6 Å, space-group P212121, and one dimer in the asymmetric unit. The crystals diffract to at least 2·8 Å resolution. Although unmodified AIDH crystallized readily, a key factor in obtaining diffraction-quality crystals was the covalent attachment of an active site reporter group, provided by 3,4-dihydro-3-methyl-6-nitro-2H-1,3-benzoxazin-2-one. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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