CRYSTALLIZATION AND PRELIMINARY-X-RAY DIFFRACTION STUDIES OF BACTERIAL RIBOSOMAL PROTEIN-L14

Citation
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
Citations number
25
Categorie Soggetti
Crystallography,Biology,"Pharmacology & Pharmacy
ISSN journal
09074449
Volume
50
Year of publication
1994
Part
5
Pages
790 - 792
Database
ISI
SICI code
0907-4449(1994)50:<790:CAPDSO>2.0.ZU;2-A
Abstract
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%.