Literature DB >> 10393302

Crystallization and preliminary crystallographic analysis of the snake muscle fructose 1,6-bisphosphatase.

D W Zhu1, G J Xu, P H Rehse, A Azzi, F K Zhao, S X Lin.   

Abstract

The snake muscle fructose 1,6-bisphosphatase, a typical allosteric enzyme which plays important roles in gluconeogenesis, was crystallized in the presence of polyethylene glycol 3350 and magnesium chloride at pH 8.5. The crystals diffract to 2.3 A on a rotating-anode X-ray source. The space group was determined to be either P3121 or its enantiomorph P3221, with unit-cell parameters a = b = 83.7, c = 202.41 A, alpha = beta = 90 and gamma = 120 degrees. There are two subunits in the asymmetric unit. Preliminary molecular-replacement studies indicate that the first enantiomorph is the correct one.

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Year:  1999        PMID: 10393302     DOI: 10.1107/s0907444999004977

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


  1 in total

1.  Association and activation of fructose 1,6-bisphosphase during unfolding and refolding: spectroscopic and enzymatic studies.

Authors:  C Yuan; Z Q Xie; F W Zhang; G J Xu
Journal:  J Protein Chem       Date:  2001-01
  1 in total

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