Literature DB >> 11468404

Crystallization and preliminary X-ray analysis of catalase-peroxidase from the halophilic archaeon Haloarcula marismortui.

Y Yamada1, S Saijo, T Sato, N Igarashi, H Usui, T Fujiwara, N Tanaka.   

Abstract

Catalase-peroxidases are bifunctional enzymes found in many microorganisms. Crystals of catalase-peroxidase from the halophilic archaeon Haloarcula marismortui were obtained using the hanging-drop vapour-diffusion method. The rhombic plate-shaped crystals were grown from purified protein solution using (NH(4))(2)SO(4) as precipitant at 293 K. The crystal belongs to the monoclinic system, space group C2, and diffracted beyond 2.0 A resolution.

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Year:  2001        PMID: 11468404     DOI: 10.1107/s0907444901008927

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


  2 in total

1.  Isonicotinic acid hydrazide conversion to Isonicotinyl-NAD by catalase-peroxidases.

Authors:  Ben Wiseman; Xavi Carpena; Miguel Feliz; Lynda J Donald; Miquel Pons; Ignacio Fita; Peter C Loewen
Journal:  J Biol Chem       Date:  2010-06-15       Impact factor: 5.157

2.  Expression, purification, crystallization and preliminary X-ray analysis of the Met244Ala variant of catalase-peroxidase (KatG) from the haloarchaeon Haloarcula marismortui.

Authors:  Tomomi Ten-I; Takashi Kumasaka; Wataru Higuchi; Satoru Tanaka; Katsuhiko Yoshimatsu; Taketomo Fujiwara; Takao Sato
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2007-10-24
  2 in total

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