Myoglobin

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Myoglobin is the first protein to be given its three-dimensional structure by X-ray crystallography; a feat achieved by John C. Kendrew, George Bodo, Harry M. Dintzis, Robert G. Parrish, Henry Wyckoff and Dorothy Crowfoot Hodgkin in 1958. The landmark paper appeared in Nature under the title "A Three-Dimensional Model of the Myoglobin Molecule Obtained by X-Ray Analysis" (volume 181, issue 4610, pages 662-6). Kendrew's pioneering work earned him half of the 1962 Nobel Prize in Chemistry, which he shared with Max Perutz. Myoglobin is an oxygen and iron binding protein found in muscle tissue of most vertebrates and almost all mammals. An STL file containing a cartoon representation of the protein with heme group residues depicted as spheres (green) and a separate file for the heme group (red) is available from the Protein Data Bank under the accession number 1MBN. The model was created using VMD software. A successfully printed model has been realized using MakerBot Replicator2 with MakerWare 2.2.2.89 and standard resolution, consisting of three shells and 25% infill, employing rafts and supports.