1pp3

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(New page: 200px<br /><applet load="1pp3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pp3, resolution 1.60&Aring;" /> '''Structure of thaumat...)
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[[Image:1pp3.gif|left|200px]]<br /><applet load="1pp3" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1pp3.gif|left|200px]]<br /><applet load="1pp3" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1pp3, resolution 1.60&Aring;" />
caption="1pp3, resolution 1.60&Aring;" />
'''Structure of thaumatin in a hexagonal space group'''<br />
'''Structure of thaumatin in a hexagonal space group'''<br />
==Overview==
==Overview==
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The intensely sweet protein thaumatin has been crystallized in a hexagonal, lattice after a temperature shift from 293 to 277 K. The structure of the, protein in the new crystal was solved at 1.6 A resolution. The protein, fold is identical to that found in three other crystal forms grown in the, presence of crystallizing agents of differing chemical natures. The, proportions of lattice interactions involving hydrogen bonds, hydrophobic, or ionic groups differ greatly from one form to another. Moreover, the, distribution of acidic and basic residues taking part in contacts also, varies. The hexagonal packing is characterized by the presence of channels, parallel to the c axis that are so wide that protein molecules can diffuse, through them.
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The intensely sweet protein thaumatin has been crystallized in a hexagonal lattice after a temperature shift from 293 to 277 K. The structure of the protein in the new crystal was solved at 1.6 A resolution. The protein fold is identical to that found in three other crystal forms grown in the presence of crystallizing agents of differing chemical natures. The proportions of lattice interactions involving hydrogen bonds, hydrophobic or ionic groups differ greatly from one form to another. Moreover, the distribution of acidic and basic residues taking part in contacts also varies. The hexagonal packing is characterized by the presence of channels parallel to the c axis that are so wide that protein molecules can diffuse through them.
==About this Structure==
==About this Structure==
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1PP3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thaumatococcus_daniellii Thaumatococcus daniellii]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PP3 OCA].
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1PP3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thaumatococcus_daniellii Thaumatococcus daniellii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PP3 OCA].
==Reference==
==Reference==
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[[Category: plant protein]]
[[Category: plant protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:59:18 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:31:01 2008''

Revision as of 12:31, 21 February 2008


1pp3, resolution 1.60Å

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Structure of thaumatin in a hexagonal space group

Overview

The intensely sweet protein thaumatin has been crystallized in a hexagonal lattice after a temperature shift from 293 to 277 K. The structure of the protein in the new crystal was solved at 1.6 A resolution. The protein fold is identical to that found in three other crystal forms grown in the presence of crystallizing agents of differing chemical natures. The proportions of lattice interactions involving hydrogen bonds, hydrophobic or ionic groups differ greatly from one form to another. Moreover, the distribution of acidic and basic residues taking part in contacts also varies. The hexagonal packing is characterized by the presence of channels parallel to the c axis that are so wide that protein molecules can diffuse through them.

About this Structure

1PP3 is a Single protein structure of sequence from Thaumatococcus daniellii. Full crystallographic information is available from OCA.

Reference

Structure of thaumatin in a hexagonal space group: comparison of packing contacts in four crystal lattices., Charron C, Giege R, Lorber B, Acta Crystallogr D Biol Crystallogr. 2004 Jan;60(Pt 1):83-9. Epub 2003 Dec, 18. PMID:14684896

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