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

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 tetrag...

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Veröffentlicht in:Journal of molecular biology 1993-09, Vol.233 (1), p.167-169
Hauptverfasser: Miki, Kunio, Tamada, Taro, Nishida, Hirokazu, Inaka, Koji, Yasui, Akira, de Ruiter, Petra E., Eker, Andre P.M.
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Sprache:eng
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Zusammenfassung: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 P4 12 12 or P 4 32 12 with unit cell dimensions of a = b = 90·7 Å and c = 135 Å. Assuming that the asymmetric unit contains one molecule, the V m value is calculated as 2·6 Å 3/dalton. The crystals are stable towards X-ray exposure and diffract beyond 2·5 Å resolution.
ISSN:0022-2836
1089-8638
DOI:10.1006/jmbi.1993.1492