C. Davies et al., CRYSTALLIZATION AND PRELIMINARY-X-RAY DIFFRACTION STUDIES OF BACTERIAL RIBOSOMAL PROTEIN-L14, Acta crystallographica. Section D, Biological crystallography, 50, 1994, pp. 790-792
Based on amino-acid sequence homology, it is predicted that ribosomal
protein L14 is a member of a recently identified family of structurall
y related RNA-binding proteins. To verify this, the gene for Bacillus
stearothermophilus L14 has been cloned, and the protein has been purif
ied and crystallized. The crystals are in space group C2 with cell dim
ensions a = 67.0, b = 32.7, c = 49.4 angstrom, and beta = 101.8-degree
s, and there is one molecule in the asymmetric unit (V(m) = 2.0 angstr
om 3 Da-1). They are of high quality, and a native data set has been c
ollected to a resolution of 1.6 angstrom with an R(merge) of 5.3%.