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

H Wang; H Yokota; R Kim; S H Kim

doi:10.1107/S0907444998007513

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

Acta Crystallogr D Biol Crystallogr. 1999 Jan;55(Pt 1):338-40. doi: 10.1107/S0907444998007513. Epub 1999 Jan 1.

Authors

H Wang¹, H Yokota, R Kim, S H Kim

Affiliation

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

PMID: 10089444
DOI: 10.1107/S0907444998007513

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.

Publication types

Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

Archaeal Proteins / chemistry*
Archaeal Proteins / genetics
Archaeal Proteins / isolation & purification*
Base Sequence
Chromosomal Proteins, Non-Histone / chemistry*
Chromosomal Proteins, Non-Histone / genetics
Chromosomal Proteins, Non-Histone / isolation & purification*
Crystallization
Crystallography, X-Ray
DNA Primers / genetics
Escherichia coli / genetics
Gene Expression
Methanococcus / chemistry*
Methanococcus / genetics
Recombinant Proteins / chemistry
Recombinant Proteins / genetics
Recombinant Proteins / isolation & purification

Substances

Archaeal Proteins
Chromosomal Proteins, Non-Histone
DNA Primers
Recombinant Proteins
fibrillarin