NDLI: Incorporation of Selenomethionine into Induced Intracytoplasmic Membrane Proteins of Rhodobacter species

Content Provider	Springer Nature Link
Author	Laible, Philip D. Hata, Aaron N. Crawford, Adam E. Hanson, Deborah K.
Copyright Year	2005
Abstract	Efficient multiple- or single-wavelength anomalous dispersion (MAD/SAD) techniques that use tunable X-ray sources at third-generation synchrotrons exploit the anomalous scattering of certain heavy atoms for determination of experimental phases. Development of methods for the in vivo substitution of methionine by selenomethionine (SeMet) has revolutionized the process for determination of structures of soluble proteins in recent years. Herein, we report methods for biosynthetic incorporation of SeMet into induced intracytoplasmic membrane proteins of two species of the Rhodobacter genus of purple non-sulfur photosynthetic bacteria. Amino acid analysis of a membrane protein complex that was purified to homogeneity determined that the extent of SeMet incorporation was extensive and approached quantitative replacement. Diffraction-quality crystals were obtained from SeMet-labeled membrane proteins purified from 2 l of culture. These methods augment the potential utility of photosynthetic bacteria and their inducible membrane systems for the production of foreign membrane proteins for structure determination.
Starting Page	95
Ending Page	102
Page Count	8
File Format	PDF
ISSN	1345711X
Journal	Journal of Structural and Functional Genomics
Volume Number	6
Issue Number	2-3
e-ISSN	15700267
Language	English
Publisher	Kluwer Academic Publishers
Publisher Date	2005-01-01
Publisher Place	Dordrecht
Access Restriction	Subscribed
Subject Keyword	autoinduction feedback inhibition Heavy-atom derivative MAD/SAD oxygen tension S-adenosyl-L-methionine Human Genetics Bioinformatics Microbial Genetics and Genomics Plant Genetics & Genomics Animal Genetics and Genomics Biochemistry
Content Type	Text
Resource Type	Article
Subject	Genetics Structural Biology Biochemistry

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