1rsm: Difference between revisions

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

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

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~~'''~~THE 2-ANGSTROMS RESOLUTION STRUCTURE OF A THERMOSTABLE RIBONUCLEASE A CHEMICALLY CROSS-LINKED BETWEEN LYSINE RESIDUES 7 AND 41~~'''~~

===THE 2-ANGSTROMS RESOLUTION STRUCTURE OF A THERMOSTABLE RIBONUCLEASE A CHEMICALLY CROSS-LINKED BETWEEN LYSINE RESIDUES 7 AND 41===

~~==Overview==~~

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The ~~crystal structure of Lys-7-~~(~~dinitrophenylene)-Lys-41-cross-linked ribonuclease A has been determined by molecular replacement and refined by restrained least-squares methods to an R factor of 0.18~~ at 2.~~0-A resolution~~. ~~Diffraction intensity data were collected by using a conventional diffractometer and an x-ray area detector. Comparison of the thermostable cross-linked protein and~~ the ~~native enzyme shows them to be structurally similar, with a rms difference in backbone and side-chain atoms of 0~~.52 and 1.34 A, respectively. Native and modified proteins additionally show 35 common bound solvent sites and similar overall temperature factor behavior, despite localized differences resulting from cross-~~link introduction, altered crystal pH, or lattice interactions with neighboring molecules. These results are discussed in the context of proposals on the origins of thermostability in the cross~~-~~linked enzyme.~~

The line below this paragraph, {{ABSTRACT_PUBMED_3936036}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 3936036 is the PubMed ID number.

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==About this Structure==

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[[Category: Sheriff, S.]]

[[Category: Weber, P C.]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 07~~:51:32 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 11:50:48 2008''

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-[[Image:1rsm.gif|left|200px]]
+{{Seed}}
+[[Image:1rsm.png|left|200px]]
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 {{STRUCTURE_1rsm|  PDB=1rsm  |  SCENE=  }}
-'''THE 2-ANGSTROMS RESOLUTION STRUCTURE OF A THERMOSTABLE RIBONUCLEASE A CHEMICALLY CROSS-LINKED BETWEEN LYSINE RESIDUES 7 AND 41'''
+===THE 2-ANGSTROMS RESOLUTION STRUCTURE OF A THERMOSTABLE RIBONUCLEASE A CHEMICALLY CROSS-LINKED BETWEEN LYSINE RESIDUES 7 AND 41===
-==Overview==
+<!--
-The crystal structure of Lys-7-(dinitrophenylene)-Lys-41-cross-linked ribonuclease A has been determined by molecular replacement and refined by restrained least-squares methods to an R factor of 0.18 at 2.0-A resolution. Diffraction intensity data were collected by using a conventional diffractometer and an x-ray area detector. Comparison of the thermostable cross-linked protein and the native enzyme shows them to be structurally similar, with a rms difference in backbone and side-chain atoms of 0.52 and 1.34 A, respectively. Native and modified proteins additionally show 35 common bound solvent sites and similar overall temperature factor behavior, despite localized differences resulting from cross-link introduction, altered crystal pH, or lattice interactions with neighboring molecules. These results are discussed in the context of proposals on the origins of thermostability in the cross-linked enzyme.
+The line below this paragraph, {{ABSTRACT_PUBMED_3936036}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 3936036 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_3936036}}
 ==About this Structure==
@@ Line 28: / Line 32: @@
 [[Category: Sheriff, S.]]
 [[Category: Weber, P C.]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 07:51:32 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 11:50:48 2008''