1z0t
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(New page: 200px<br /><applet load="1z0t" size="450" color="white" frame="true" align="right" spinBox="true" caption="1z0t, resolution 3.00Å" /> '''Crystal Structure of...)
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Revision as of 05:03, 21 November 2007
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Crystal Structure of A. fulgidus Lon proteolytic domain
Overview
Although macromolecular crystallography is rapidly becoming largely, routine owing to advances in methods of data collection, structure, solution and refinement, difficult cases are still common. To remind, structural biologists about the kinds of crystallographic difficulties, that might be encountered, case studies of several successfully completed, structure determinations that utilized less than perfect crystals are, discussed here. The structure of the proteolytic domain of Archaeoglobus, fulgidus Lon was solved with crystals that contained superimposed, orthorhombic and monoclinic lattices, a case not previously described for, proteins. Another hexagonal crystal form of this protein exhibited an, unusually high degree of non-isomorphism. Crystals of A. fulgidus Rio1, kinase exhibited both pseudosymmetry and twinning. Ways of identifying the, observed phenomena and approaches to solving and refining macromolecular, structures when only less than perfect crystals are available are, discussed here.
About this Structure
1Z0T is a Single protein structure of sequence from Archaeoglobus fulgidus. Active as Endopeptidase La, with EC number 3.4.21.53 Full crystallographic information is available from OCA.
Reference
Pathological crystallography: case studies of several unusual macromolecular crystals., Dauter Z, Botos I, LaRonde-LeBlanc N, Wlodawer A, Acta Crystallogr D Biol Crystallogr. 2005 Jul;61(Pt 7):967-75. Epub 2005, Jun 24. PMID:15983420
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