Literature DB >> 15299380

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

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

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%.

Entities:  

Year:  1994        PMID: 15299380     DOI: 10.1107/S0907444994004117

Source DB:  PubMed          Journal:  Acta Crystallogr D Biol Crystallogr        ISSN: 0907-4449


  2 in total

1.  Circular Permutation Obscures Universality of a Ribosomal Protein.

Authors:  Nicholas A Kovacs; Petar I Penev; Amitej Venapally; Anton S Petrov; Loren Dean Williams
Journal:  J Mol Evol       Date:  2018-10-10       Impact factor: 2.395

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

Authors:  Heng Dong; Dandan Liu; Tianyu Han; Yuxue Zhao; Ji Sun; Sue Lin; Jiashu Cao; Zhong-Hua Chen; Li Huang
Journal:  Sci Rep       Date:  2015-11-24       Impact factor: 4.379

  2 in total

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