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Methods Enzymol. 2021;659:71-103. doi: 10.1016/bs.mie.2021.07.006. Epub 2021 Sep 25.

Purification, reconstitution, and mass analysis of archaeal RNase P, a multisubunit ribonucleoprotein enzyme.

Methods in enzymology

Walter J Zahurancik, Andrew S Norris, Stella M Lai, Dalton T Snyder, Vicki H Wysocki, Venkat Gopalan

Affiliations

  1. Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH, United States; Center for RNA Biology, The Ohio State University, Columbus, OH, United States.
  2. Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH, United States; Center for RNA Biology, The Ohio State University, Columbus, OH, United States; Resource for Native Mass Spectrometry-Guided Structural Biology, The Ohio State University, Columbus, OH, United States.
  3. Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH, United States; Resource for Native Mass Spectrometry-Guided Structural Biology, The Ohio State University, Columbus, OH, United States.
  4. Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH, United States; Center for RNA Biology, The Ohio State University, Columbus, OH, United States; Resource for Native Mass Spectrometry-Guided Structural Biology, The Ohio State University, Columbus, OH, United States. Electronic address: [email protected].
  5. Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH, United States; Center for RNA Biology, The Ohio State University, Columbus, OH, United States. Electronic address: [email protected].

PMID: 34752299 DOI: 10.1016/bs.mie.2021.07.006

Abstract

The ubiquitous ribonucleoprotein (RNP) form of RNase P catalyzes the Mg

Copyright © 2021 Elsevier Inc. All rights reserved.

Keywords: Mass photometry; Mass spectrometry; Protein modification; Protein oligomerization; Ribonucleoprotein

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