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Crystallization and preliminary X-ray crystallographic study of ribosome-inactivating protein from barley seeds (1994)

Song, H. K. ; Hwang, K. Y. ; Kim, K. K. ; [et al.]

Copenhagen : International Union of Crystallography (IUCr)

Acta crystallographica 50 (1994), S. 910-912

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ISSN: 1399-0047

Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001

Topics: Chemistry and Pharmacology , Geosciences , Physics

Notes: 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 Å and β = 108.62°. The asymmetric unit contains one molecule of ribosome-inactivating protein with a corresponding crystal volume per protein mass (Vm) of 2.32 Å3 Da−1 and a solvent content of 47% by volume. The crystal diffracts to about 2.3 Å 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 Å Bragg spacing) have been collected from a native crystal.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1107/S0907444994002544

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