Crystallization and Preliminary X-ray Diffraction Studies of Photolyase (Photoreactivating Enzyme) from the Cyanobacterium Anacystis nidulans

Kunio Miki, Taro Tamada, Hirokazu Nishida, Koji Inaka, Akira Yasui, Petra E. de Ruiter, Andre P.M. Eker

Research output: Contribution to journalArticlepeer-review

18 Citations (Scopus)

Abstract

Photolyase (photoreactivating enzyme) from the cyanobacterium Anacystis nidulans was crystallized by the hanging drop vapor diffusion procedure using ammonium sulfate as a precipitant. The pale-yellow crystals were grown to a size of 0·4 mm in length and 0·1 mm in diameter. They belong to the tetragonal space group P41212 or P 43212 with unit cell dimensions of a = b = 90·7 AÅ and c = 135 Å. Assuming that the asymmetric unit contains one molecule, the Vm value is calculated as 2·6 Å3/dalton. The crystals are stable towards X-ray exposure and diffract beyond 2·5 AÅ resolution.

Original languageEnglish
Pages (from-to)167-169
Number of pages3
JournalJournal of Molecular Biology
Volume233
Issue number1
DOIs
Publication statusPublished - 1993 Sep 1
Externally publishedYes

Keywords

  • DNA photoreactivating enzyme
  • DNA repair
  • Photolyase
  • Protein crystallization
  • X-ray diffraction

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Molecular Biology

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