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Publication Abstract from PubMed

Two orthorhombic forms (Vm values are 2.3 and 3.0 A3/Da) of bovine beta-trypsin crystals in neat cyclohexane were determined to 1.93 A resolution, by X-ray diffraction. Both structures in organic solvent are similar to those in aqueous solution. In the high packing density form, one cyclohexane molecule is found in a hydrophobic site near the active center. One sulfate locates at the active site with hydrogen or salt bond to the Ser-His catalytic diad, and five more sulfates bind on the molecular surface. The conformation of the side chains near the sulfates changed greatly. In the low packing density form, one cyclohexane and three sulfates are found. In both structures, one benzamidine molecule locates at the hydrophobic pocket of the active center. Most water molecules on the enzyme surface are retained except some with high temperature factors.

X-ray studies on two forms of bovine beta-trypsin crystals in neat cyclohexane.,Zhu G, Huang Q, Wang Z, Qian M, Jia Y, Tang Y Biochim Biophys Acta. 1998 Dec 8;1429(1):142-50. PMID:9920392^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.