Literature DB >> 12925800

Overproduction, crystallization and preliminary X-ray diffraction analysis of probable ATP sulfurylase from Thermus thermophilus HB8.

Yuichi Taguchi1, Jun Hoseki, Yoshimitsu Kakuta, Keiichi Fukuyama.   

Abstract

ATP sulfurylase catalyzes the reaction of inorganic sulfate with ATP, producing adenosine-5'-phosphosulfate (APS) and pyrophosphate. A probable ATP sulfurylase (MW = 38.8 kDa) from Thermus thermophilus HB8 was overproduced in Escherichia coli and purified. It was crystallized in the presence of 5 mM APS by the batch method. The crystal was monoclinic, space group P2(1), with unit-cell parameters a = 68.8, b = 61.2, c = 128.6 A, beta = 95.4 degrees. Diffraction to better than 2.5 A resolution was obtained using synchrotron radiation at SPring-8. The asymmetric unit most probably contains two subunits (V(M) = 3.48 A(3) Da(-1)).

Entities:  

Mesh:

Substances:

Year:  2003        PMID: 12925800     DOI: 10.1107/s0907444903014641

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


  2 in total

1.  Purification, crystallization and preliminary X-ray diffraction analysis of adenosine triphosphate sulfurylase (ATPS) from the sulfate-reducing bacterium Desulfovibrio desulfuricans ATCC 27774.

Authors:  Olga Yu Gavel; Anna V Kladova; Sergey A Bursakov; João M Dias; Susana Texeira; Valery L Shnyrov; José J G Moura; Isabel Moura; Maria J Romão; José Trincão
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2008-06-07

2.  Cloning, expression and bioinformatics analysis of ATP sulfurylase from Acidithiobacillus ferrooxidans ATCC 23270 in Escherichia coli.

Authors:  Michael L Jaramillo; Michel Abanto; Ruth L Quispe; Julio Calderón; Luís J Del Valle; Miguel Talledo; Pablo Ramírez
Journal:  Bioinformation       Date:  2012-08-03
  2 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.