1ce2

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{{STRUCTURE_1ce2| PDB=1ce2 | SCENE= }}
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'''STRUCTURE OF DIFERRIC BUFFALO LACTOFERRIN AT 2.5A RESOLUTION'''
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===STRUCTURE OF DIFERRIC BUFFALO LACTOFERRIN AT 2.5A RESOLUTION===
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==Overview==
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The structure of buffalo lactoferrin has been determined at 303 K. The crystals belong to orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 77.5, b = 91.0, c = 131.5 A and Z = 4. The structure has been refined to an R factor of 0.187. The overall structure of the protein is similar to its structure determined at 277 K in a different crystal form. However, the lobe orientations in the two structures differ by 9.0 degrees, suggesting significant inter-lobe flexibility in this family of proteins. The inter-lobe interactions are predominantly hydrophobic and could act as a cushion for a change in orientation under the influence of external conditions. On the other hand, the domain arrangements are found to be similar in 277 and 303 K crystal structures, with orientations differing by 1.5 and 1.0 degrees in the N and C lobes, respectively. The results of these investigations suggest that the increase in temperature helps in the production of better quality crystals.
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{{ABSTRACT_PUBMED_10531476}}
==About this Structure==
==About this Structure==
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[[Category: Room temperature]]
[[Category: Room temperature]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:36:56 2008''

Revision as of 17:36, 30 June 2008

Image:1ce2.png

Template:STRUCTURE 1ce2

STRUCTURE OF DIFERRIC BUFFALO LACTOFERRIN AT 2.5A RESOLUTION

Template:ABSTRACT PUBMED 10531476

About this Structure

1CE2 is a Single protein structure of sequence from Bubalus bubalis. Full crystallographic information is available from OCA.

Reference

Structure of buffalo lactoferrin at 2.5 A resolution using crystals grown at 303 K shows different orientations of the N and C lobes., Karthikeyan S, Paramasivam M, Yadav S, Srinivasan A, Singh TP, Acta Crystallogr D Biol Crystallogr. 1999 Nov;55(Pt 11):1805-13. PMID:10531476

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