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Journal Articles Acta Crystallographica Section D: Biological Crystallography Year : 2003

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

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.

Dates and versions

hal-04145156 , version 1 (28-06-2023)

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Anne-Laure Gall, Marc Ruff, Dino Moras. The dual role of CHAPS in the crystallization of stromelysin-3 catalytic domain. Acta Crystallographica Section D: Biological Crystallography, 2003, 59 (Pt 3), pp.603-606. ⟨10.1107/s0907444902017870⟩. ⟨hal-04145156⟩
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