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Atomic resolution structure of native porcine pancreatic elastase at 1.1 Å by Martin Würtele; Michael Hahn; Kai Hilpert; Wolfgang Höhne is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.
What is Atomic resolution structure of native porcine pancreatic elastase at 1.1 Å about?
A data set from the serine protease porcine pancreatic elastase was collected at atomic resolution (1.1 A Ê ) 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 1 H atom was located at a distance of 0.82 A Ê from the N 1 atom. The distance between His57 N 1 and Asp102 O 2 is 2.70 AE 0.04 A Ê , thus indicating normal hydrogen-bonding geometry. Additional H atoms at His57 N 42 and Ser195 O could not be identi®ed in the F o À F c density maps.
Who reads Atomic resolution structure of native porcine pancreatic elastase at 1.1 Å?
It is typically read by researchers, students, and practitioners in Biochemistry, Genetics and Molecular Biology.
- Author
- Martin Würtele; Michael Hahn; Kai Hilpert; Wolfgang Höhne
- Publisher
- International Union of Crystallography; Blackwell Publishing Inc.; International Union of Crystallography (IUCr) (ISSN 0907-4449)
- Published
- 2000
- Language
- EN
- Field
- Biochemistry, Genetics and Molecular Biology (Life Sciences)