title: Crystallization and preliminary X-ray diffraction studies of trypsin-like proteases from the gastric fluid of the marine crab Cancer pagurus.
abstract: The digestive fluid of the marine crab Cancer pagurus (Decapoda, Brachyura) contains highly stable proteases which display enhanced activity in aqueous mixtures of organic solvents. Three trypsins were isolated from the gastric fluid and two of them, C.p.TryII and C.p.TryIII, were purified to homogeneity by anion-exchange chromatography and crystallized by hanging-drop vapour diffusion. Diffraction data were collected at a synchrotron to 0.97 and 3.2 A resolution, respectively. The crystal of C.p.TryII belongs to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 52.06, b = 62.00, c = 71.66 A. Based on the Matthews coefficient, one protein molecule per asymmetric unit is suggested. In contrast, crystals of C.p.TryIII, which belong to the cubic space group P2(1)3 with unit-cell parameters a = b = c = 215.4 A, are assumed to contain 12 molecules per asymmetric unit.
authors.affiliation: Institute of Biochemistry and Molecular Biology, University of Hamburg, 20146 Hamburg, Germany.
authors.forename: Jan-Hendrik
authors.initials: JH
authors.lastname: Hehemann
authors.forename: Lars
authors.initials: L
authors.lastname: Redecke
authors.forename: Markus
authors.initials: M
authors.lastname: Perbandt
authors.forename: Reinhard
authors.initials: R
authors.lastname: Saborowski
authors.forename: Christian
authors.initials: C
authors.lastname: Betzel
mesh_terms: D000818:Animals; D003386:Brachyura / Q000201:enzymology*; D003460:Crystallization; D005750:Gastric Juice / Q000201:enzymology*; D010447:Peptide Hydrolases / Q000737:chemistry* / Q000302:isolation & purification; D014357:Trypsin / Q000737:chemistry* / Q000302:isolation & purification; D014961:X-Ray Diffraction / Q000379:methods*
chemical_list: D010447:Peptide Hydrolases; D014357:Trypsin