Ribosome‐inactivating protein from barley seeds has been crystallized using polyethylene glycol as precipitant. The crystal belongs to the monoclinic space groupC2, with unit‐cell parametersa= 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−1and 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
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