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

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 stearothermophUus 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/~, and ,8 = 101.8 °, and there is one molecule in the asymmetric unit (V,,, = 2.0 A 3 Da -~). They are of high quality, and a native data set has been collected to a resolution of 1.6 t%, with an emerge of 5.3%.

Diversification and evolution of the SDG gene family in Brassica rapa after the whole genome triplication

“…On the other hand, the gaining AT-hook, which binds proteins to the AT-rich DNA sequences, was identified in three SUVH proteins. Moreover, several domains were detected in SDG proteins for the first time, including the helix-hairpin-helix1 (HhH1) DNA-binding domain and the iron-sulphur binding domain (FES) finding in DNA lyase 23 24 in one Trx protein and Ribosomal-14 domain for RNA binding and Stress-antifung domain for stress tolerance and antifungal activity 25 26 27 in two SUVR proteins ( Tables S5 and S6 ).…”