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 |
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Format: | Artikel |
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. |
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ISSN: | 0022-2836 1089-8638 |
DOI: | 10.1006/jmbi.1993.1492 |