Literature DB >> 2380985

Crystallization and preliminary X-ray crystallographic studies of benzamidine-inhibited trypsin from the North Atlantic salmon (Salmo salar).

A O Smalås1, A Hordvik, L K Hansen, E Hough, K Jynge.   

Abstract

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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Year:  1990        PMID: 2380985     DOI: 10.1016/0022-2836(90)90185-o

Source DB:  PubMed          Journal:  J Mol Biol        ISSN: 0022-2836            Impact factor:   5.469


  2 in total

Review 1.  Atlantic cod trypsins: from basic research to practical applications.

Authors:  Agústa Gudmundsdóttir; Helga Margrét Pálsdóttir
Journal:  Mar Biotechnol (NY)       Date:  2005-02-17       Impact factor: 3.619

2.  Differences in PAR-2 activating potential by king crab (Paralithodes camtschaticus), salmon (Salmo salar), and bovine (Bos taurus) trypsin.

Authors:  Anett K Larsen; Kurt Kristiansen; Ingebrigt Sylte; Ole-Morten Seternes; Berit E Bang
Journal:  BMC Res Notes       Date:  2013-07-20
  2 in total

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