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ABSTRACT:
SUBMITTER: Beich-Frandsen M
PROVIDER: S-EPMC3087635 | biostudies-literature | 2011 May
REPOSITORIES: biostudies-literature
Beich-Frandsen Mads M Večerek Branislav B Sjöblom Björn B Bläsi Udo U Djinović-Carugo Kristina K
Acta crystallographica. Section F, Structural biology and crystallization communications 20110420 Pt 5
The structure of full-length host factor Qβ (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 Å, α = 78.6, β = 86.2, γ = 59.9°, was solved by molecular replacement to a resolution of 2.85 Å 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 ~65% of the fu ...[more]