Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 402, Issue 1, Pages 154-164Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2010.07.017
Keywords
RNA; ribonucleoprotein particle; crystallisation; crystallography; tertiary interaction
Categories
Funding
- Medical Research Council
- Human Frontier Science Program
- National Science and Engineering Research Council of Canada
- ORS Fund
- Cambridge Commonwealth Trust
- Sidney Sussex College
- MRC [MC_U105184330] Funding Source: UKRI
- Medical Research Council [MC_U105184330] Funding Source: researchfish
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RNA is known to perform diverse roles in the cell, often as ribonucleoprotein (RNP) particles. While the crystal structure of these RNP particles could provide crucial insights into their functions, crystallographic work on RNP complexes is often hampered by difficulties in obtaining well-diffracting crystals. The small nuclear ribonucleoprotein (snRNP) core domain, acting as an assembly nucleus for the maturation of snRNPs, plays a crucial role in the biogenesis of four of the spliceosomal snRNPs. We have succeeded in crystallising the human U4 snRNP core domain containing seven Sm proteins and a truncated U4 snRNA variant. The most critical factor in our success in the crystallisation was the introduction of various tertiary interaction modules into the RNA that could promote crystal packing without altering the core structure. Here, we describe various strategies employed in our crystallisation effort that could be applied to crystallisation of other RNP particles. (C) 2010 Elsevier Ltd. All rights reserved.
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