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2eql

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{{STRUCTURE_2eql| PDB=2eql | SCENE= }}
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'''CRYSTALLOGRAPHIC STUDIES OF A CALCIUM BINDING LYSOZYME FROM EQUINE MILK AT 2.5 ANGSTROMS RESOLUTION'''
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===CRYSTALLOGRAPHIC STUDIES OF A CALCIUM BINDING LYSOZYME FROM EQUINE MILK AT 2.5 ANGSTROMS RESOLUTION===
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==Overview==
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The crystal structure of a calcium binding equine lysozyme has been determined at 2.5 A resolution by means of molecular replacement. The energy minimized equine lysozyme as the starting model, was refined with the molecular dynamics program, X-PLOR, and the R factor of the current model was found to be 24% without any water molecules. The conformation of the calcium binding loop is similar to that of alpha-lactalbumin. The profiles of backbone atomic displacements throughout the lysozyme and alpha-lactalbumin superfamilies are comparable as well as their homologous tertiary structures.
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(as it appears on PubMed at http://www.pubmed.gov), where 1569037 is the PubMed ID number.
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{{ABSTRACT_PUBMED_1569037}}
==About this Structure==
==About this Structure==
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[[Category: Miyano, M.]]
[[Category: Miyano, M.]]
[[Category: Tsuge, H.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 18:42:33 2008''

Revision as of 15:42, 27 July 2008

Image:2eql.png

Template:STRUCTURE 2eql

CRYSTALLOGRAPHIC STUDIES OF A CALCIUM BINDING LYSOZYME FROM EQUINE MILK AT 2.5 ANGSTROMS RESOLUTION

Template:ABSTRACT PUBMED 1569037

About this Structure

2EQL is a Single protein structure of sequence from Equus caballus. Full crystallographic information is available from OCA.

Reference

Crystallographic studies of a calcium binding lysozyme from equine milk at 2.5 A resolution., Tsuge H, Ago H, Noma M, Nitta K, Sugai S, Miyano M, J Biochem. 1992 Feb;111(2):141-3. PMID:1569037

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