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

Wang H, Yokota H, Kim R, Kim SH



Published 1999-02-01 in Acta Crystallogr D Biol Crystallogr volume 55 .

Pubmed ID: 10089444
DOI identifier: -

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.


This publication refers to following proteins:



Last modification of this entry: Sept. 6, 2012