1hix: Difference between revisions

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

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

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~~'''~~CRYSTALLOGRAPHIC ANALYSES OF FAMILY 11 ENDO-BETA-1,4-XYLANASE XYL1 FROM STREPTOMYCES SP. S38~~'''~~

===CRYSTALLOGRAPHIC ANALYSES OF FAMILY 11 ENDO-BETA-1,4-XYLANASE XYL1 FROM STREPTOMYCES SP. S38===

~~==Overview==~~

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~~Family 11 endo~~-~~beta~~-1,~~4-xylanases degrade xylan~~, the main constituent of plant hemicelluloses, and have many potential uses in biotechnology. The structure of Xyl1, a family 11 endo-xylanase from Streptomyces sp. S38, has been solved. The protein crystallized from ammonium sulfate in the ~~trigonal space group P321, with unit-cell parameters a = b = 71.49, c = 130.30 A, gamma = 120.0 degrees. The structure was solved~~ at ~~2.0 A by X-ray crystallography using the molecular-replacement method and refined to a final R factor of 18~~.~~5% (R(free) = 26~~.9%)~~. Xyl1 has the overall fold characteristic of family 11 xylanases~~, ~~with two highly twisted beta-sheets defining a long cleft containing~~ the ~~two catalytic residues Glu87 and Glu177~~.

The line below this paragraph, {{ABSTRACT_PUBMED_11717493}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 11717493 is the PubMed ID number.

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==About this Structure==

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[[Category: Hydrolase]]

[[Category: Xylan degradation]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ ~~2 18~~:53:19 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:14:41 2008''

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-[[Image:1hix.gif|left|200px]]
+{{Seed}}
+[[Image:1hix.png|left|200px]]
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 {{STRUCTURE_1hix|  PDB=1hix  |  SCENE=  }}
-'''CRYSTALLOGRAPHIC ANALYSES OF FAMILY 11 ENDO-BETA-1,4-XYLANASE XYL1 FROM STREPTOMYCES SP. S38'''
+===CRYSTALLOGRAPHIC ANALYSES OF FAMILY 11 ENDO-BETA-1,4-XYLANASE XYL1 FROM STREPTOMYCES SP. S38===
-==Overview==
+<!--
-Family 11 endo-beta-1,4-xylanases degrade xylan, the main constituent of plant hemicelluloses, and have many potential uses in biotechnology. The structure of Xyl1, a family 11 endo-xylanase from Streptomyces sp. S38, has been solved. The protein crystallized from ammonium sulfate in the trigonal space group P321, with unit-cell parameters a = b = 71.49, c = 130.30 A, gamma = 120.0 degrees. The structure was solved at 2.0 A by X-ray crystallography using the molecular-replacement method and refined to a final R factor of 18.5% (R(free) = 26.9%). Xyl1 has the overall fold characteristic of family 11 xylanases, with two highly twisted beta-sheets defining a long cleft containing the two catalytic residues Glu87 and Glu177.
+The line below this paragraph, {{ABSTRACT_PUBMED_11717493}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11717493 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11717493}}
 ==About this Structure==
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 [[Category: Hydrolase]]
 [[Category: Xylan degradation]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 18:53:19 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 08:14:41 2008''