| Literature DB >> 15358374 |
David M Mueller1, Neeti Puri, Venkataraman Kabaleeswaran, Cassandra Terry, Andrew G W Leslie, John E Walker.
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.Entities:
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Year: 2004 PMID： 15358374 DOI： 10.1016/j.pep.2004.06.035
Source DB: PubMed Journal: Protein Expr Purif ISSN： 1046-5928 Impact factor: 1.650