Crystallization and preliminary X-ray diffraction studies of bacterial ribosomal protein L14

C Davies; S E Gerchman; J H Kycia; K McGee; V Ramakrishnan; S W White

doi:10.1107/S0907444994004117

Crystallization and preliminary X-ray diffraction studies of bacterial ribosomal protein L14

Acta Crystallogr D Biol Crystallogr. 1994 Sep 1;50(Pt 5):790-2. doi: 10.1107/S0907444994004117.

Authors

C Davies¹, S E Gerchman, J H Kycia, K McGee, V Ramakrishnan, S W White

Affiliation

¹ Department of Microbiology, Duke University Medical Centre, Durham, North Carolina 27710, USA.

PMID: 15299380
DOI: 10.1107/S0907444994004117

Abstract

Based on amino-acid sequence homology, it is predicted that ribosomal protein L14 is a member of a recently identified family of structurally related RNA-binding proteins. To verify this, the gene for Bacillus stearothermophilus L14 has been cloned, and the protein has been purified and crystallized. The crystals are in space group C2 with cell dimensions a = 67.0, b = 32.7, c = 49.4 A, and beta = 101.8 degrees, and there is one molecule in the asymmetric unit (V(m) = 2.0 A(3) Da(-1)). They are of high quality, and a native data set has been collected to a resolution of 1.6 A, with an R(merge) of 5.3%.