Literature DB >> 18221022

Purification, crystallization and preliminary X-ray studies of AxCesD required for efficient cellulose biosynthesis in Acetobacter xylinum.

SongQing Hu1, YongGui Gao, Kenji Tajima, Min Yao, Takanori Yoda, Daisuke Shimura, Yasuharu Satoh, Shin Kawano, Isao Tanaka, Masanobu Munekata.   

Abstract

AxCesD protein required for bacterial cellulose biosynthesis in Acetobacter xylinum was overexpressed in E. coli, purified and crystallized. Single crystals of SeMet-substituted AxCesD were obtained by the sitting-drop vapor-diffusion method. The crystal belongs to the primitive trigonal space group P3 2, with unit-cell parameters a = b = 77.7 A, and c = 213.9 A. The asymmetric unit in the crystal was assumed to contain 8 protein molecules giving the Matthews coefficient (VM) of 2.54 A3 Da(-1). Se-MAD data were collected to 2.3 A resolution using synchrotron radiations.

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Year:  2008        PMID: 18221022     DOI: 10.2174/092986608783330422

Source DB:  PubMed          Journal:  Protein Pept Lett        ISSN: 0929-8665            Impact factor:   1.890


  1 in total

1.  Characterization of pellicle inhibition in Gluconacetobacter xylinus 53582 by a small molecule, pellicin, identified by a chemical genetics screen.

Authors:  Janice L Strap; Andrew Latos; Isaac Shim; Dario T Bonetta
Journal:  PLoS One       Date:  2011-12-09       Impact factor: 3.240

  1 in total

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