1z0v

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[[Image:1z0v.gif|left|200px]]
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{{STRUCTURE_1z0v| PDB=1z0v | SCENE= }}
{{STRUCTURE_1z0v| PDB=1z0v | SCENE= }}
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'''Crystal Structure of A. fulgidus Lon proteolytic domain'''
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===Crystal Structure of A. fulgidus Lon proteolytic domain===
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==Overview==
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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.
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The line below this paragraph, {{ABSTRACT_PUBMED_15983420}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 15983420 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15983420}}
==About this Structure==
==About this Structure==
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==Reference==
==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:[http://www.ncbi.nlm.nih.gov/pubmed/15983420 15983420]
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:[http://www.ncbi.nlm.nih.gov/pubmed/15983420 15983420]
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Atomic-resolution crystal structure of the proteolytic domain of Archaeoglobus fulgidus lon reveals the conformational variability in the active sites of lon proteases., Botos I, Melnikov EE, Cherry S, Kozlov S, Makhovskaya OV, Tropea JE, Gustchina A, Rotanova TV, Wlodawer A, J Mol Biol. 2005 Aug 5;351(1):144-57. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16002085 16002085]
[[Category: Archaeoglobus fulgidus]]
[[Category: Archaeoglobus fulgidus]]
[[Category: Endopeptidase La]]
[[Category: Endopeptidase La]]
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[[Category: B-type lon]]
[[Category: B-type lon]]
[[Category: Catalytic ser-lys dyad]]
[[Category: Catalytic ser-lys dyad]]
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Revision as of 09:13, 28 July 2008

Template:STRUCTURE 1z0v

Crystal Structure of A. fulgidus Lon proteolytic domain

Template:ABSTRACT PUBMED 15983420

About this Structure

1Z0V is a Single protein structure of sequence from Archaeoglobus fulgidus. 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

Atomic-resolution crystal structure of the proteolytic domain of Archaeoglobus fulgidus lon reveals the conformational variability in the active sites of lon proteases., Botos I, Melnikov EE, Cherry S, Kozlov S, Makhovskaya OV, Tropea JE, Gustchina A, Rotanova TV, Wlodawer A, J Mol Biol. 2005 Aug 5;351(1):144-57. PMID:16002085

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