1ly0: Difference between revisions

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New page: left|200px<br /><applet load="1ly0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ly0, resolution 1.36Å" /> '''Structure of thaumat...
 
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[[Image:1ly0.jpg|left|200px]]<br /><applet load="1ly0" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1ly0.jpg|left|200px]]<br /><applet load="1ly0" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1ly0, resolution 1.36&Aring;" />
caption="1ly0, resolution 1.36&Aring;" />
'''Structure of thaumatin crystallized in the presence of glycerol'''<br />
'''Structure of thaumatin crystallized in the presence of glycerol'''<br />


==Overview==
==Overview==
The intensely sweet protein thaumatin has been crystallized at 293 K in, the presence of sodium tartrate and 25%(v/v) glycerol for X-ray, diffraction data collection at 100 K. A comparison of the, three-dimensional structure model derived from a crystal grown in the, presence of glycerol with that of a control deprived of this additive, reveals only minor changes in the overall structure but a approximately, 20% reduction in the number of water molecules. X-ray topography analyses, show that the overall quality of the crystals prepared in the presence of, this cryoprotectant is enhanced.
The intensely sweet protein thaumatin has been crystallized at 293 K in the presence of sodium tartrate and 25%(v/v) glycerol for X-ray diffraction data collection at 100 K. A comparison of the three-dimensional structure model derived from a crystal grown in the presence of glycerol with that of a control deprived of this additive reveals only minor changes in the overall structure but a approximately 20% reduction in the number of water molecules. X-ray topography analyses show that the overall quality of the crystals prepared in the presence of this cryoprotectant is enhanced.


==About this Structure==
==About this Structure==
1LY0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thaumatococcus_daniellii Thaumatococcus daniellii] with TLA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LY0 OCA].  
1LY0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thaumatococcus_daniellii Thaumatococcus daniellii] with <scene name='pdbligand=TLA:'>TLA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LY0 OCA].  


==Reference==
==Reference==
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[[Category: Kadri, A.]]
[[Category: Kadri, A.]]
[[Category: Lorber, B.]]
[[Category: Lorber, B.]]
[[Category: Robert, M.C.]]
[[Category: Robert, M C.]]
[[Category: TLA]]
[[Category: TLA]]
[[Category: sweet protein]]
[[Category: sweet protein]]
[[Category: taste-modifying protein]]
[[Category: taste-modifying protein]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:58:20 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:49:33 2008''

Revision as of 14:49, 21 February 2008

File:1ly0.jpg


1ly0, resolution 1.36Å

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Structure of thaumatin crystallized in the presence of glycerol

OverviewOverview

The intensely sweet protein thaumatin has been crystallized at 293 K in the presence of sodium tartrate and 25%(v/v) glycerol for X-ray diffraction data collection at 100 K. A comparison of the three-dimensional structure model derived from a crystal grown in the presence of glycerol with that of a control deprived of this additive reveals only minor changes in the overall structure but a approximately 20% reduction in the number of water molecules. X-ray topography analyses show that the overall quality of the crystals prepared in the presence of this cryoprotectant is enhanced.

About this StructureAbout this Structure

1LY0 is a Single protein structure of sequence from Thaumatococcus daniellii with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Crystallization in the presence of glycerol displaces water molecules in the structure of thaumatin., Charron C, Kadri A, Robert MC, Giege R, Lorber B, Acta Crystallogr D Biol Crystallogr. 2002 Dec;58(Pt 12):2060-5. Epub 2002, Nov 23. PMID:12454465

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