| Chapter title |
Structural Studies of Matrix Metalloproteinase by X-Ray Diffraction
|
|---|---|
| Chapter number | 4 |
| Book title |
Matrix Metalloproteases
|
| Published in |
Methods in molecular biology, March 2017
|
| DOI | 10.1007/978-1-4939-6863-3_4 |
| Pubmed ID | |
| Book ISBNs |
978-1-4939-6861-9, 978-1-4939-6863-3
|
| Authors |
Elena Decaneto, Wolfgang Lubitz, Hideaki Ogata |
| Editors |
Charles A. Galea |
| 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. |
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