Structural highlights
Publication Abstract from PubMed
The structure of full-length host factor Qbeta (Hfq) from Escherichia coli obtained from a crystal belonging to space group P1, with unit-cell parameters a = 61.91, b = 62.15, c = 81.26 A, alpha = 78.6, beta = 86.2, gamma = 59.9 degrees , was solved by molecular replacement to a resolution of 2.85 A and refined to R(work) and R(free) values of 20.7% and 25.0%, respectively. Hfq from E. coli has previously been crystallized and the structure has been solved for the N-terminal 72 amino acids, which cover approximately 65% of the full-length sequence. Here, the purification, crystallization and structural data of the full 102-amino-acid protein are presented. These data revealed that the presence of the C-terminus changes the crystal packing of E. coli Hfq. The crystal structure is discussed in the context of the recently published solution structure of Hfq from E. coli.
Structural analysis of full-length Hfq from Escherichia coli.,Beich-Frandsen M, Vecerek B, Sjoblom B, Blasi U, Djinovic-Carugo K Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 May 1;67(Pt, 5):536-40. Epub 2011 Apr 20. PMID:21543856[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Beich-Frandsen M, Vecerek B, Sjoblom B, Blasi U, Djinovic-Carugo K. Structural analysis of full-length Hfq from Escherichia coli. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 May 1;67(Pt, 5):536-40. Epub 2011 Apr 20. PMID:21543856 doi:10.1107/S174430911100786X
