1cgt: Difference between revisions

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[[Image:1cgt.~~gif~~|left|200px]]

[[Image:1cgt.png|left|200px]]

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~~'''~~STRUCTURE OF CYCLODEXTRIN GLYCOSYLTRANSFERASE REFINED AT 2.0 ANGSTROMS RESOLUTION~~'''~~

===STRUCTURE OF CYCLODEXTRIN GLYCOSYLTRANSFERASE REFINED AT 2.0 ANGSTROMS RESOLUTION===

~~==Overview==~~

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The ~~previously reported structural model of cyclodextrin glycosyltransferase (EC 2.4.1.19) from Bacillus circulans has been improved. For~~ this ~~purpose~~ the ~~known sequence was built into an electron density map established by multiple isomorphous replacement and subsequent solvent-flattening~~ at 2.~~5 A resolution~~. ~~The resulting model was refined at 2.0 A resolution using a simulated annealing refinement method. Based on 70~~,~~171 independent reflections in~~ the ~~range 7~~.~~0 to 2.0 A resolution, a final R~~-factor of 17.6% was obtained with a model obeying standard geometry within 0.013 A in bond lengths and 2.7 degrees in bond angles. The final model consists of all 684 amino acid residues, two calcium ions and 588 solvent molecules.

The line below this paragraph, {{ABSTRACT_PUBMED_1826034}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 1826034 is the PubMed ID number.

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==About this Structure==

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[[Category: Schulz, G E.]]

[[Category: Glycosyltransferase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May 2 12~~:43:17 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:43:48 2008''

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-[[Image:1cgt.gif|left|200px]]
+{{Seed}}
+[[Image:1cgt.png|left|200px]]
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 {{STRUCTURE_1cgt|  PDB=1cgt  |  SCENE=  }}
-'''STRUCTURE OF CYCLODEXTRIN GLYCOSYLTRANSFERASE REFINED AT 2.0 ANGSTROMS RESOLUTION'''
+===STRUCTURE OF CYCLODEXTRIN GLYCOSYLTRANSFERASE REFINED AT 2.0 ANGSTROMS RESOLUTION===
-==Overview==
+<!--
-The previously reported structural model of cyclodextrin glycosyltransferase (EC 2.4.1.19) from Bacillus circulans has been improved. For this purpose the known sequence was built into an electron density map established by multiple isomorphous replacement and subsequent solvent-flattening at 2.5 A resolution. The resulting model was refined at 2.0 A resolution using a simulated annealing refinement method. Based on 70,171 independent reflections in the range 7.0 to 2.0 A resolution, a final R-factor of 17.6% was obtained with a model obeying standard geometry within 0.013 A in bond lengths and 2.7 degrees in bond angles. The final model consists of all 684 amino acid residues, two calcium ions and 588 solvent molecules.
+The line below this paragraph, {{ABSTRACT_PUBMED_1826034}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 1826034 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_1826034}}
 ==About this Structure==
@@ Line 26: / Line 30: @@
 [[Category: Schulz, G E.]]
 [[Category: Glycosyltransferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 12:43:17 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:43:48 2008''