Literature DB >> 15299742

Crystallization and preliminary X-ray crystallographic analysis of recombinant transaldolase B from Eschericha coli.

J Jia1, Y Lindqvist, G Schneider, U Schörken, H Sahm, G A Sprenger.   

Abstract

Recombinant transaldolase from Escherichia coli, an enzyme of the pentose phosphate pathway has been crystallized by the vapor-diffusion method using polyethylene glycol 6000 as precipitant. The crystals are orthorhombic, space group P2(1)2(1)2(1) with cell dimensions a = 68.9, b = 91.3 and c = 130.5 A and diffract to 2 A resolution on a conventional X-ray source. The asymmetric unit very likely contains two subunits, corresponding to a packing density of 2.9 A(3) Da(-1).

Entities:  

Year:  1996        PMID: 15299742     DOI: 10.1107/S0907444995010365

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


  1 in total

1.  Crystallization and preliminary X-ray diffraction analysis of transaldolase from Thermoplasma acidophilum.

Authors:  Anja Lehwess-Litzmann; Piotr Neumann; Ralph Golbik; Christoph Parthier; Kai Tittmann
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2011-04-27
  1 in total

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