Journal
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
Volume 56, Issue -, Pages 520-523Publisher
MUNKSGAARD INT PUBL LTD
DOI: 10.1107/S0907444900000299
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A data set from the serine protease porcine pancreatic elastase was collected at atomic resolution (1.1 Angstrom) with synchrotron radiation. The improved resolution allows the determination of atom positions with high accuracy, as well as the localization of H atoms. Three residues could be modelled in alternative positions. The catalytic triad of elastase consists of His57, Asp102 and Ser195. The His57 N-delta 1 H atom was located at a distance of 0.82 Angstrom from the N-delta 1 atom. The distance between His57 N-delta 1 and Asp102 O-delta 2 is 2.70 +/- 0.04 Angstrom, thus indicating normal hydrogen-bonding geometry. Additional H atoms at His57 N-epsilon 2 and Ser195 O-gamma could not be identified in the F-o - F-c density maps.
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