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          Institute: MPI für bioanorganische Chemie     Collection: MPI für bioanorganische Chemie     Display Documents



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ID: 733850.0, MPI für bioanorganische Chemie / MPI für bioanorganische Chemie
Structural Studies of Matrix Metalloproteinase by X-Ray Diffraction.
Authors:Decaneto, Elena; Lubitz, Wolfgang; Ogata, Hideaki
Language:English
Date of Publication (YYYY-MM-DD):2017
Title of Journal:Methods Molecular Biology
Journal Abbrev.:Methods Mol.Biol.
Volume:1579
Start Page:49
End Page:60
Review Status:Internal review
Audience:Experts Only
Abstract / Description: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.
Comment of the Author/Creator:Date: 2017, 2017
External Publication Status:published
Document Type:Article
Communicated by:N. N.
Affiliations:MPI für bioanorganische Chemie
Identifiers:ISI:28299732 [ID No:1]
ISSN:1064-3745 [ID No:2]
DOI:10.1007/978-1-4939-6863-3_4 [ID No:3]
ISBN:9781493968619 [ID No:4]
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