Figure 23.4.4.4

Mattos, C.; Ringe, D.

doi:10.1107/97809553602060000717

International
Tables for
Crystallography
Volume F
Crystallography of biological macromolecules
Edited by M. G. Rossmann and E. Arnold

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International Tables for Crystallography (2006). Vol. F. ch. 23.4, p. 633 | 1 | 2 |

Figure 23.4.4.4

C. Mattos^a ^* and D. Ringe^b

^aDepartment of Molecular and Structural Biochemistry, North Carolina State University, 128 Polk Hall, Raleigh, NC 02795, USA, and ^bRosenstiel Basic Medical Sciences Research Center, Brandeis University, 415 South St, Waltham, MA 02254, USA
Correspondence e-mail: [email protected]

Figure 23.4.4.4

Crystal structure of porcine pancreatic elastase represented as a ribbon diagram using MOLSCRIPT (Kraulis, 1991). The two α-helices are shown in green, the β-sheets are in purple and the coils are in grey. Elastase contains 240 amino-acid residues, and is composed of two β-barrel domains. The catalytic triad (Asp108, His60 and Ser203) is shown explicitly. The buried crystallographic water molecules found in 11 superimposed elastase structures solved in a variety of solvents are shown in red.