Bibliographic Details
| 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] |
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| Database: |
Engineering Source |
