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The dual role of CHAPS in the crystallization of stromelysin-3 catalytic domain.

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Title: The dual role of CHAPS in the crystallization of stromelysin-3 catalytic domain.
Authors: Gall, Anne-Laure, Ruff, Marc, Moras, Dino
Source: Acta Crystallographica: Section D (Wiley-Blackwell). Mar2003, Vol. 59 Issue 3, p603. 4p.
Subjects: Proteins, Crystallization
Abstract: CHAPS {3-[(3-cholamidopropyl) dimethylammonio]-1-propane sulfonate} is a non-denaturing detergent widely used for protein solubilization and stabilization. CHAPS was used to avoid protein aggregation during concentration of the recombinant stromelysin-3 (ST3) catalytic domain and was required to stabilize the protein, allowing its crystallization. The crystal structure of the complex between the ST3 catalytic domain and a phosphinic inhibitor shows two CHAPS molecules binding to ST3 in two different orientations. One CHAPS molecule is masking a hydrophobic surface of the protein, thus avoiding protein aggregation. This detergent molecule is also involved in packing interactions. The other detergent molecule is located in a pocket formed by the N- and C-terminal parts of the ST3 and stabilizes a loop that normally binds a Ca atom. [ABSTRACT FROM AUTHOR]
Copyright of Acta Crystallographica: Section D (Wiley-Blackwell) is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
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  Data: The dual role of CHAPS in the crystallization of stromelysin-3 catalytic domain.
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  Data: <searchLink fieldCode="AR" term="%22Gall%2C+Anne-Laure%22">Gall, Anne-Laure</searchLink><br /><searchLink fieldCode="AR" term="%22Ruff%2C+Marc%22">Ruff, Marc</searchLink><br /><searchLink fieldCode="AR" term="%22Moras%2C+Dino%22">Moras, Dino</searchLink>
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  Data: CHAPS {3-[(3-cholamidopropyl) dimethylammonio]-1-propane sulfonate} is a non-denaturing detergent widely used for protein solubilization and stabilization. CHAPS was used to avoid protein aggregation during concentration of the recombinant stromelysin-3 (ST3) catalytic domain and was required to stabilize the protein, allowing its crystallization. The crystal structure of the complex between the ST3 catalytic domain and a phosphinic inhibitor shows two CHAPS molecules binding to ST3 in two different orientations. One CHAPS molecule is masking a hydrophobic surface of the protein, thus avoiding protein aggregation. This detergent molecule is also involved in packing interactions. The other detergent molecule is located in a pocket formed by the N- and C-terminal parts of the ST3 and stabilizes a loop that normally binds a Ca atom. [ABSTRACT FROM AUTHOR]
– Name: AbstractSuppliedCopyright
  Label:
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  Data: <i>Copyright of Acta Crystallographica: Section D (Wiley-Blackwell) is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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        Value: 10.1107/S0907444902017870
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