Literature DB >> 17768357

Purification, crystallization and preliminary X-ray analysis of the fumarylacetoacetase family member TTHA0809 from Thermus thermophilus HB8.

Hisashi Mizutani1, Naoki Kunishima.   

Abstract

Fumarylacetoacetase catalyzes the final step of tyrosine and phenylalanine catabolism. A recombinant form of the fumarylacetoacetase family member TTHA0809 from Thermus thermophilus HB8 has been crystallized by the oil-microbatch method using sodium chloride as a precipitating agent. The crystals belong to the monoclinic space group P2(1), with unit-cell parameters a = 93.3, b = 73.4, c = 122.6 A, beta = 111.8 degrees. The crystals are most likely to contain two dimers in the asymmetric unit, with a V(M) value of 3.32 A3 Da(-1). Diffraction data were collected at 2.2 A resolution using synchrotron radiation at beamline BL26B1 of SPring-8, Japan.

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Year:  2007        PMID: 17768357      PMCID: PMC2376325          DOI: 10.1107/S1744309107039590

Source DB:  PubMed          Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun        ISSN: 1744-3091


  8 in total

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8.  How to measure and predict the molar absorption coefficient of a protein.

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  8 in total
  1 in total

1.  Expression, Purification, Crystallization, and Enzyme Assays of Fumarylacetoacetate Hydrolase Domain-Containing Proteins.

Authors:  Alexander K H Weiss; Max Holzknecht; Elia Cappuccio; Ilaria Dorigatti; Karin Kreidl; Andreas Naschberger; Bernhard Rupp; Hubert Gstach; Pidder Jansen-Dürr
Journal:  J Vis Exp       Date:  2019-06-20       Impact factor: 1.355

  1 in total

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