期刊
PROTEIN EXPRESSION AND PURIFICATION
卷 37, 期 2, 页码 479-485出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.pep.2004.06.035
关键词
mitochondrion; ATPase; ATP synthase; crystallization
类别
资金
- FIC NIH HHS [1F06TW002379] Funding Source: Medline
- NIGMS NIH HHS [R01-GM067091, R01-GM066233] Funding Source: Medline
The yeast mitochondrial ATPase has been genetically modified to include a HiS(6) Ni-affinity tag on the amino end of the mature P-subunit. The modified beta-subunit is imported into the mitochondrion, properly processed to the mature form, and assembled into a mature and fully active ATP synthase. The F-1-ATPase has been purified from submitochondrial particles after release from the membrane with chloroform, followed by Ni-chelate-affinity and gel filtration chromatography. The final enzyme is a homogeneous preparation with full activity and no apparent degradation products. This enzyme preparation has been used to obtain crystals that diffract to better than 2.8 Angstrom resolution. (C) 2004 Elsevier Inc. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据