Crystallization and preliminary X-ray crystallographic analysis of the catalytic domain of membrane type 1 matrix metalloproteinase

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Abstract

Membrane type 1 matrix metalloproteinase (MT1-MMP) belongs to the large family of zinc-dependent endopeptidases termed MMPs that are located in the extracellular matrix. MT1-MMP was crystallized at 277 K using the vapour-diffusion method with PEG as a precipitating agent. Data sets for MT1-MMP were collected to 2.24 Å resolution at 100 K. The crystals belonged to space group P43212, with unit-cell parameters a = 62.99, c = 122.60 Å. The crystal contained one molecule per asymmetric unit, with a Matthews coefficient (V M) of 2.90 Å3 Da-1; the solvent content is estimated to be 57.6%. © 2014 International Union of Crystallography All rights reserved.

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Ogata, H., Decaneto, E., Grossman, M., Havenith, M., Sagi, I., Lubitz, W., & Knipp, M. (2014). Crystallization and preliminary X-ray crystallographic analysis of the catalytic domain of membrane type 1 matrix metalloproteinase. Acta Crystallographica Section F:Structural Biology Communications, 70(2), 232–235. https://doi.org/10.1107/S2053230X13034857

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