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Title
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Crystallization and preliminary X-ray crystallographic studies of benzamidine-inhibited trypsin from the North Atlantic salmon (Salmo salar).
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Authors
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A.O.Smalås,
A.Hordvik,
L.K.Hansen,
E.Hough,
K.Jynge.
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Ref.
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J Mol Biol, 1990,
214,
355-358.
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PubMed id
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Abstract
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Crystals of benzamidine-inhibited trypsin from the North Atlantic salmon (Salmo
salar) have been grown from ammonium sulphate solution at pH 5.0. Two crystal
forms suitable for X-ray structure analysis, obtained from a hanging-drop
experiment, have been characterized. Both belong to space-group P22(1)2(1) with
cell dimensions a = 39.2 A, b = 62.4 A, c = 84.6 A and a = 31.4 A, b = 74.8 A, c
= 83.5 A, for forms I and II, respectively. Intensity data to 1.82 A have been
collected for crystal form I on a CAD4 diffractometer, and initial phases have
been obtained by molecular replacement methods. The conventional R-factor after
two rounds of model building and subsequent refinement is 0.25 for data between
6.0 and 2.0 A. So far no water molecules have been included in the model.
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