1igp: Difference between revisions

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

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

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~~'''~~X-RAY CRYSTALLOGRAPHIC STUDIES OF RECOMBINANT INORGANIC PYROPHOSPHATASE FROM ESCHERICHIA COLI~~'''~~

===X-RAY CRYSTALLOGRAPHIC STUDIES OF RECOMBINANT INORGANIC PYROPHOSPHATASE FROM ESCHERICHIA COLI===

~~==Overview==~~

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~~An E. coli inorganic pyrophosphatase overproducer and a method for a large-scale production of the homogeneous enzyme are described.~~ The ~~inorganic pyrophosphatase was crystallized in the form containing one subunit of a homohexameric molecule per asymmetric unit: space group R32~~, ~~a = 110.4 A~~, ~~c = 76.8 A. The electron density map~~ to ~~2.5 A resolution phased with Eu- and Hg-derivatives~~ (~~figure of merit, <m> = 0~~.~~51) was improved by the solvent flattening procedure (<m> = 0~~.77)~~. The course of the polypeptide chain and the secondary structure elements~~, ~~intersubunit contacts and positions of~~ the ~~active sites were characterized. Homology with S. cerevisiae inorganic pyrophosphatase structure was found~~.

The line below this paragraph, {{ABSTRACT_PUBMED_8034059}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 8034059 is the PubMed ID number.

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==About this Structure==

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[[Category: Oganessyan, V Yu.]]

[[Category: Acid anhydride hydrolase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ ~~2 19~~:58:38 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 11:59:48 2008''

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-[[Image:1igp.gif|left|200px]]
+{{Seed}}
+[[Image:1igp.png|left|200px]]
 <!--
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 {{STRUCTURE_1igp|  PDB=1igp  |  SCENE=  }}
-'''X-RAY CRYSTALLOGRAPHIC STUDIES OF RECOMBINANT INORGANIC PYROPHOSPHATASE FROM ESCHERICHIA COLI'''
+===X-RAY CRYSTALLOGRAPHIC STUDIES OF RECOMBINANT INORGANIC PYROPHOSPHATASE FROM ESCHERICHIA COLI===
-==Overview==
+<!--
-An E. coli inorganic pyrophosphatase overproducer and a method for a large-scale production of the homogeneous enzyme are described. The inorganic pyrophosphatase was crystallized in the form containing one subunit of a homohexameric molecule per asymmetric unit: space group R32, a = 110.4 A, c = 76.8 A. The electron density map to 2.5 A resolution phased with Eu- and Hg-derivatives (figure of merit, &lt;m&gt; = 0.51) was improved by the solvent flattening procedure (&lt;m&gt; = 0.77). The course of the polypeptide chain and the secondary structure elements, intersubunit contacts and positions of the active sites were characterized. Homology with S. cerevisiae inorganic pyrophosphatase structure was found.
+The line below this paragraph, {{ABSTRACT_PUBMED_8034059}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 8034059 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_8034059}}
 ==About this Structure==
@@ Line 27: / Line 31: @@
 [[Category: Oganessyan, V Yu.]]
 [[Category: Acid anhydride hydrolase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 19:58:38 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 11:59:48 2008''