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Acta Crystallogr D Biol Crystallogr. 1999 Jan;55(Pt 1):338-40. Epub 1999 Jan 1.

Expression, purification and preliminary X-ray analysis of a fibrillarin homolog from Methanococcus jannaschii, a hyperthermophile.

Author information

1
Department of Chemistry and Physical Biosciences Division, Lawrence Berkeley National Laboratory, University of California Berkeley, Berkeley, CA 94720-5230, USA.

Abstract

Fibrillarin plays a central role in ribosome biogenesis as a ribosomal RNA-processing protein. A Methanococcus jannaschii homolog of fibrillarin has been overexpressed, purified and crystallized. Crystals belong to the C2 space group with unit-cell parameters a = 121.4, b = 43.2, c = 55.3 A, beta = 96.9 degrees. Under flash-frozen conditions and using synchrotron radiation, the crystals diffract to 1.8 A resolution. For structural determination, a selenomethionine derivative of the protein has also been crystallized.

PMID:
10089444
DOI:
10.1107/S0907444998007513
[Indexed for MEDLINE]

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