2ojr: Difference between revisions

Revision as of 09:51, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2ojr.png

Template:STRUCTURE 2ojr

Structure of ubiquitin solved by SAD using the Lanthanide-Binding TagStructure of ubiquitin solved by SAD using the Lanthanide-Binding Tag

Template:ABSTRACT PUBMED 17497863

About this StructureAbout this Structure

2OJR is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Double-lanthanide-binding tags for macromolecular crystallographic structure determination., Silvaggi NR, Martin LJ, Schwalbe H, Imperiali B, Allen KN, J Am Chem Soc. 2007 Jun 6;129(22):7114-20. Epub 2007 May 12. PMID:17497863

Page seeded by OCA on Mon Jul 28 09:51:37 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:2ojr.jpg|left|200px]]
+{{Seed}}
+[[Image:2ojr.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_2ojr|  PDB=2ojr  |  SCENE=  }}
-'''Structure of ubiquitin solved by SAD using the Lanthanide-Binding Tag'''
+===Structure of ubiquitin solved by SAD using the Lanthanide-Binding Tag===
-==Overview==
+<!--
-A double-lanthanide-binding tag (dLBT), a small peptide sequence engineered to bind two lanthanide ions (e.g., Tb3+) with high affinity, was used to solve the phase problem for the structure determination of ubiquitin by the single-wavelength anomalous diffraction (SAD) method. Since the dLBT is comprised exclusively of encoded amino acids, the necessity for the incorporation of unnatural amino acids or chemical modification of the protein as a prerequisite for X-ray structure determination is eliminated. A construct encoding the dLBT as an N-terminal fusion with ubiquitin provides for facile expression and purification using standard methods. Phasing of the single-wavelength X-ray data (at 2.6 A resolution) using only the anomalous signal from the two tightly bound Tb3+ ions in the dLBT led to clear electron-density maps. Nearly 75% of the ubiquitin structure was built using automated model-building software without user intervention. It is anticipated that this technique will be broadly applicable, complementing existing macromolecular phasing methodologies. The dLBT should be particularly useful in cases where protein derivatization with heavy atoms proves to be problematic or synchrotron facilities are unavailable.
+The line below this paragraph, {{ABSTRACT_PUBMED_17497863}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17497863 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17497863}}
 ==About this Structure==
@@ Line 28: / Line 32: @@
 [[Category: Tb]]
 [[Category: Terbium]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 11:03:29 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 09:51:37 2008''