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2 citations found for Rester, U.
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The complex formed between the antistasin-type inhibitor bdellastasin and porcine β-trypsin has been crystallized in the tetragonal crystal form of space group P41212 and solved and refined to 2.7 Å resolution. A comparison with the porcine β-trypsin–bdellastasin complex of the enantiomorphic space group P43212 and other known crystal structures of porcine β-trypsin–macromolecular inhibitor complexes suggests that deamidation, isomerization and racemization of trypsin residue Asn115 is the key step in its crystallization.
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The synthetic gene of the amino-terminal domain of the antistasin-type inhibitor ghilanten (ghilanten-D1) from H. ghilianii was constructed, expressed in the methylotrophic yeast P. pastoris and purified by heparin–Sepharose chromatography. Recombinant ghilanten-D1 has been crystallized in complex with porcine β-trypsin in three different-looking but isomorphous crystal forms, each belonging to the orthorhombic space group P212121.