Literature DB >> 11264599

Purification, crystallization and preliminary X-ray studies of thermostable alkaline phosphatase from Thermus sp. 3041.

C N Ji1, T Jiang, M Q Chen, X Y Sheng, Y M Mao.   

Abstract

Thermostable alkaline phosphatase from Thermus sp. 3041 has been expressed in Escherichia coli, purified and crystallized. The crystals belong to space group P2(1)22(1), with unit-cell parameters a = 57.7, b = 69.9, c = 111.5 A. Diffraction data were collected to 2.54 A with a completeness of 91.1% (87.8% for the last shell), an R(merge) value of 0.105 (0.312) and an I/sigma(I) value of 9.5 (3.6).

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Year:  2001        PMID: 11264599     DOI: 10.1107/s0907444901001226

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


  1 in total

1.  Cloning of an alkaline phosphatase gene from the moderately thermophilic bacterium Meiothermus ruber and characterization of the recombinant enzyme.

Authors:  J V Yurchenko; A V Budilov; S M Deyev; I S Khromov; A Y Sobolev
Journal:  Mol Genet Genomics       Date:  2003-08-19       Impact factor: 3.291

  1 in total

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