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. 2011 Dec 1;67(Pt 12):1516-8.
doi: 10.1107/S1744309111045131. Epub 2011 Nov 30.

Crystallization and preliminary X-ray structure analysis of human ribosomal protein L30e

Akiko Kawaguchi  1 , Toyoyuki Ose, Min Yao, Isao Tanaka
Affiliations

Crystallization and preliminary X-ray structure analysis of human ribosomal protein L30e

Akiko Kawaguchi et al. Acta Crystallogr Sect F Struct Biol Cryst Commun. .

Abstract

Many functions have been reported for the eukaryotic ribosomal protein L30e. L30e makes several inter-subunit and intra-subunit interactions with protein or RNA components of the 80S ribosome. Yeast L30e has been shown to bind to its own transcript to autoregulate expression at both the transcriptional and the translational levels. Furthermore, it has been reported that mammalian L30e is a component of the selenocysteine-incorporation machinery by binding to the selenocysteine-insertion sequence on mRNA. As high-resolution crystal structures of mammalian L30e are not available, the purification, crystallization and X-ray structure analysis of human L30e are presented here.

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Figures

Figure 1
Figure 1
Crystal of human L30e.
Figure 2
Figure 2
Cartoon representation of human L30e. Specific intramolecular interactions that are not observed in yeast L30e are shown with amino-acid residues in stick representation and hydrogen bonds as black dashed lines.
See this image and copyright information in PMC

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