Crystallization and preliminary X-ray crystallographic studies of benzamidine-inhibited trypsin from the North Atlantic salmon (Salmo salar).
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.
Smalås
A O
AO
Department of Chemistry, University of Tromsø, Norway.
Hordvik
A
A
Hansen
L K
LK
Hough
E
E
Jynge
K
K
D000578:Amidines / Q000494:pharmacology*; D000595:Amino Acid Sequence; D000818:Animals; D001550:Benzamidines / Q000494:pharmacology*; D003460:Crystallization; D008969:Molecular Sequence Data; D012474:Salmon; D012689:Sequence Homology, Nucleic Acid; D014357:Trypsin; D014361:Trypsin Inhibitors / Q000494:pharmacology; D014961:X-Ray Diffraction
D000578:Amidines; D001550:Benzamidines; D014361:Trypsin Inhibitors; D014357:Trypsin; C032157:benzamidine