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The structure of ribosomal protein L1 from M. thermolithotrophicus compared with L1 protein structures from two other sources reveals two regions which retain their structure in all three proteins. These structural invariants are involved in intermolecular interactions in the crystals and could be treated as potential RNA-binding sites.
research papers
Different complexes of ribosomal proteins with specific rRNA fragments have been crystallized and studied by our group during the last six years. There are several factors important for successful crystallization of RNA/protein complexes, among them: length and content of RNA fragments, homogeneity of RNA and protein preparations, stability of the complexes, conditions for mixing RNA and protein components before crystallization, effect of Se-Met on RNA/protein complex crystal quality. In this paper we describe findings and methodical details, which helped us to succeed in obtaining X-ray quality crystals of several RNA/protein complexes.
