Literature DB >> 11375504

Crystallization and preliminary crystallographic data of fructose-1,6-bisphosphatase from human muscle.

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

Abstract

The enzyme human muscle fructose-1,6-bisphosphatase, which plays a critical role in gluconeogenesis, has been crystallized in the presence of 2-propanol, polyethylene glycol and magnesium chloride at pH 7.5. The space group was determined to be P4(2)2(1)2, with unit-cell parameters a = b = 73.57, c = 146.50 A, alpha = beta = lambda = 90 degrees and one subunit in the asymmetric unit. A 99.6% complete data set to 2.04 A has been collected at the National Synchrotron Light Source.

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Year:  2001        PMID: 11375504     DOI: 10.1107/s0907444901004371

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


  1 in total

1.  Crystal structures of human muscle fructose-1,6-bisphosphatase: novel quaternary states, enhanced AMP affinity, and allosteric signal transmission pathway.

Authors:  Rong Shi; Ze-Yong Chen; Dao-Wei Zhu; Chunmin Li; Yufei Shan; Genjun Xu; Sheng-Xiang Lin
Journal:  PLoS One       Date:  2013-09-27       Impact factor: 3.240

  1 in total

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