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.
CITATION STYLE
Decaneto, E., Lubitz, W., & Ogata, H. (2017). Structural studies of matrix metalloproteinase by X-ray diffraction. In Methods in Molecular Biology (Vol. 1579, pp. 49–60). Humana Press Inc. https://doi.org/10.1007/978-1-4939-6863-3_4
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