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

H Ogata, E Decaneto, Moran Grossman, M Havenith, Irit Sagi, W Lubitz, M Knipp

Research output: Contribution to journalArticlepeer-review

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%.

Original languageEnglish
Pages (from-to)232-235
Number of pages4
JournalActa Crystallographica Section F-Structural Biology And Crystallization Communications
Volume70
Issue number2
DOIs
StatePublished - Feb 2014

All Science Journal Classification (ASJC) codes

  • Condensed Matter Physics
  • Genetics
  • Biophysics
  • Structural Biology
  • Biochemistry

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