1z0v
From Proteopedia
(New page: 200px<br /><applet load="1z0v" size="450" color="white" frame="true" align="right" spinBox="true" caption="1z0v, resolution 3.00Å" /> '''Crystal Structure of...) |
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| - | [[Image:1z0v.gif|left|200px]]<br /><applet load="1z0v" size=" | + | [[Image:1z0v.gif|left|200px]]<br /><applet load="1z0v" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1z0v, resolution 3.00Å" /> | caption="1z0v, resolution 3.00Å" /> | ||
'''Crystal Structure of A. fulgidus Lon proteolytic domain'''<br /> | '''Crystal Structure of A. fulgidus Lon proteolytic domain'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Although macromolecular crystallography is rapidly becoming largely | + | 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== | ==About this Structure== | ||
| - | 1Z0V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus]. Active as [http://en.wikipedia.org/wiki/Endopeptidase_La Endopeptidase La], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.53 3.4.21.53] Full crystallographic information is available from [http:// | + | 1Z0V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus]. Active as [http://en.wikipedia.org/wiki/Endopeptidase_La Endopeptidase La], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.53 3.4.21.53] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z0V OCA]. |
==Reference== | ==Reference== | ||
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[[Category: catalytic ser-lys dyad]] | [[Category: catalytic ser-lys dyad]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:11:03 2008'' |
Revision as of 14:11, 21 February 2008
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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
1Z0V 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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