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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Crystallization and preliminary X-ray crystallographic study of ribosome-inactivating protein from barley seeds.

Ribosome-inactivating protein from barley seeds has been crystallized using polyethylene glycol as precipitant. The crystal belongs to the monoclinic space group C2, with unit-cell parameters a = 88.36, b = 62.59, c = 53.18 A and beta = 108.62 degrees. The asymmetric unit contains one molecule of ribosome-inactivating protein with a corresponding crystal volume per protein mass (V(m)) of 2.32 A(3) Da(-1) and a solvent content of 47% by volume. The crystal diffracts to about 2.3 A with X-rays from a rotating-anode source and is very stable in the X-ray beam. X-ray data (nearly complete to 2.4 A Bragg spacing) have been collected from a native crystal.[1]

References

  1. Crystallization and preliminary X-ray crystallographic study of ribosome-inactivating protein from barley seeds. Song, H.K., Hwang, K.Y., Kim, K.K., Suh, S.W. Acta Crystallogr. D Biol. Crystallogr. (1994) [Pubmed]
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