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Structural Studies of Matrix Metalloproteinase by X-Ray Diffraction.

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Decaneto,  Elena
Research Department Lubitz, Max Planck Institute for Chemical Energy Conversion, Max Planck Society;

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Lubitz,  Wolfgang
Research Department Lubitz, Max Planck Institute for Chemical Energy Conversion, Max Planck Society;

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Ogata,  Hideaki
Research Department Lubitz, Max Planck Institute for Chemical Energy Conversion, Max Planck Society;

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Citation

Decaneto, E., Lubitz, W., & Ogata, H. (2017). Structural Studies of Matrix Metalloproteinase by X-Ray Diffraction. Methods in Molecular Biology, 1579, 49-60. doi:10.1007/978-1-4939-6863-3_4.


Cite as: https://hdl.handle.net/21.11116/0000-0006-E1E9-5
Abstract
Matrix Metalloproteinases (MMPs) are a family of proteolytic enzymes whose endopeptidase activity is dependent on the presence of specific metal ions. MT1-MMP (or MMP-14), which has been implicated in tumor progression and cellular invasion, contains a membrane-spanning region located C-terminal to a hemopexin-like domain and an N-terminal catalytic domain. We recombinantly expressed the catalytic domain of human MT1-MMP in E. coli and purified it from inclusion bodies using a refolding protocol that yielded significant quantities of active protein. Crystals of MT1-MMP were obtained using the vapour diffusion method. Here, we describe the protocols used for crystallization and the data analysis together with the resulting diffraction pattern.