SGD Paper 
Mueller DM, et al. (2004) Ni-chelate-affinity purification and crystallization of the yeast mitochondrial F1-ATPase. Protein Expr Purif 37(2):479-85
Abstract: The yeast mitochondrial ATPase has been genetically modified to include a His(6) Ni-affinity tag on the amino end of the mature beta-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 A resolution.
| Status: Published | Type: Journal Article | Research Support, Non-U.S. Gov't | Research Support, U.S. Gov't, Non-P.H.S. | Research Support, U.S. Gov't, P.H.S. | PubMed ID: 15358374 |
Topics addressed in this paper
Number of different genes curated to this paper: 5
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