Literature DB >> 8880936

Crystallization and preliminary X-ray diffraction studies of formylmethanofuran: tetrahydromethanopterin formyltransferase from Methanopyrus kandleri.

S Shima1, R K Thauer, H Michel, U Ermler.   

Abstract

Formylmethanofuran:tetrahydromethanopterin formyltransferase from the hyperthermophilic methanogenic Archaeon Methanopyrus kandleri (growth temperature optimum 98 degrees C) was crystallized by vapor diffusion methods. Crystal form M obtained with 2-methyl-2,4-pentanediol as precipitant displayed the space group P2(1) with unit cell parameters of a = 87.0 A, b = 75.4 A, c = 104.7 A, and beta = 113.9 degrees and diffracted better than 2 A resolution. Crystal form P grown from polyethylene glycol 8000 belonged to the space group I4(1)22 and had unit cell parameters of 157.5 A and 242.1 A. Diffraction data to 1.73 A were recorded. Crystal form S which was crystallized from (NH4)2SO4 in the space group I4(1)22 with unit cell parameters of 151.3 A and 249.5 A diffracted at least to 2.2 A resolution. All crystal forms probably have four molecules per asymmetric unit and are suitable for X-ray structure analysis.

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Year:  1996        PMID: 8880936     DOI: 10.1002/(SICI)1097-0134(199609)26:1<118::AID-PROT12>3.0.CO;2-J

Source DB:  PubMed          Journal:  Proteins        ISSN: 0887-3585


  1 in total

1.  Crystal structures and enzymatic properties of three formyltransferases from archaea: environmental adaptation and evolutionary relationship.

Authors:  Björn Mamat; Annette Roth; Clemens Grimm; Ulrich Ermler; Christos Tziatzios; Dieter Schubert; Rudolf K Thauer; Seigo Shima
Journal:  Protein Sci       Date:  2002-09       Impact factor: 6.725

  1 in total

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