1c0c

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(New page: 200px<br /><applet load="1c0c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1c0c, resolution 2.0&Aring;" /> '''BOVINE PANCREATIC RIB...)
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[[Image:1c0c.gif|left|200px]]<br /><applet load="1c0c" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1c0c.gif|left|200px]]<br /><applet load="1c0c" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1c0c, resolution 2.0&Aring;" />
caption="1c0c, resolution 2.0&Aring;" />
'''BOVINE PANCREATIC RIBONUCLEASE A DESICCATED FOR 4.0 DAYS'''<br />
'''BOVINE PANCREATIC RIBONUCLEASE A DESICCATED FOR 4.0 DAYS'''<br />
==Overview==
==Overview==
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Unlike most protein crystals, form IX of bovine pancreatic ribonuclease A, diffracts well when severely dehydrated. Crystal structures have been, solved after 2.5 and 4 days of desiccation with CaSO4, at 1.9 and 2.0 A, resolution, respectively. The two desiccated structures are very similar., An RMS displacement of 1.6 A is observed for main-chain atoms in each, structure when compared to the hydrated crystal structure with some large, rearrangements observed in loop regions. The structural changes are the, result of intermolecular contacts formed by strong electrostatic, interactions in the absence of a high dielectric medium. The electron, density is very diffuse for some surface loops, consistent with a very, disordered structure. This disorder is related to the conformational, changes. These results help explain conformational changes during the, lyophilization of protein and the associated phenomena of denaturation and, molecular memory.
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Unlike most protein crystals, form IX of bovine pancreatic ribonuclease A diffracts well when severely dehydrated. Crystal structures have been solved after 2.5 and 4 days of desiccation with CaSO4, at 1.9 and 2.0 A resolution, respectively. The two desiccated structures are very similar. An RMS displacement of 1.6 A is observed for main-chain atoms in each structure when compared to the hydrated crystal structure with some large rearrangements observed in loop regions. The structural changes are the result of intermolecular contacts formed by strong electrostatic interactions in the absence of a high dielectric medium. The electron density is very diffuse for some surface loops, consistent with a very disordered structure. This disorder is related to the conformational changes. These results help explain conformational changes during the lyophilization of protein and the associated phenomena of denaturation and molecular memory.
==About this Structure==
==About this Structure==
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1C0C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Pancreatic_ribonuclease Pancreatic ribonuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.5 3.1.27.5] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1C0C OCA].
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1C0C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Pancreatic_ribonuclease Pancreatic ribonuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.5 3.1.27.5] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C0C OCA].
==Reference==
==Reference==
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[[Category: Pancreatic ribonuclease]]
[[Category: Pancreatic ribonuclease]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Bell, J.A.]]
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[[Category: Bell, J A.]]
[[Category: SO4]]
[[Category: SO4]]
[[Category: dehydrated]]
[[Category: dehydrated]]
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[[Category: rna)]]
[[Category: rna)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:03:41 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:01:03 2008''

Revision as of 10:01, 21 February 2008


1c0c, resolution 2.0Å

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BOVINE PANCREATIC RIBONUCLEASE A DESICCATED FOR 4.0 DAYS

Overview

Unlike most protein crystals, form IX of bovine pancreatic ribonuclease A diffracts well when severely dehydrated. Crystal structures have been solved after 2.5 and 4 days of desiccation with CaSO4, at 1.9 and 2.0 A resolution, respectively. The two desiccated structures are very similar. An RMS displacement of 1.6 A is observed for main-chain atoms in each structure when compared to the hydrated crystal structure with some large rearrangements observed in loop regions. The structural changes are the result of intermolecular contacts formed by strong electrostatic interactions in the absence of a high dielectric medium. The electron density is very diffuse for some surface loops, consistent with a very disordered structure. This disorder is related to the conformational changes. These results help explain conformational changes during the lyophilization of protein and the associated phenomena of denaturation and molecular memory.

About this Structure

1C0C is a Single protein structure of sequence from Bos taurus with as ligand. Active as Pancreatic ribonuclease, with EC number 3.1.27.5 Full crystallographic information is available from OCA.

Reference

X-ray crystal structures of a severely desiccated protein., Bell JA, Protein Sci. 1999 Oct;8(10):2033-40. PMID:10548049

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