Related Experiment Video

Updated: Mar 6, 2026

Bacterial Expression and Purification of Human Matrix Metalloproteinase-3 using Affinity Chromatography
07:32

Bacterial Expression and Purification of Human Matrix Metalloproteinase-3 using Affinity Chromatography

Published on: March 30, 2022

5.2K

Structural Studies of Matrix Metalloproteinase by X-Ray Diffraction

Elena Decaneto1, Wolfgang Lubitz1, Hideaki Ogata2

  • 1Max Planck Institute for Chemical Energy Conversion, Stiftstrasse 34-36, 45470, Mülheim an der Ruhr, Germany.

Methods in Molecular Biology (Clifton, N.J.)
|March 17, 2017
PubMed

Insights

Researchers successfully produced and crystallized the catalytic domain of Matrix Metalloproteinase-14 (MT1-MMP), an enzyme linked to cancer invasion. This work provides a foundation for understanding MT1-MMP structure and function.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Matrix Metalloproteinases (MMPs) are zinc-dependent endopeptidases.
  • MT1-MMP (MMP-14) plays a role in tumor progression and cellular invasion.
  • MT1-MMP possesses a catalytic domain, a hemopexin-like domain, and a membrane-spanning region.

Purpose of the Study:

  • To express and purify the catalytic domain of human MT1-MMP.
  • To develop protocols for crystallizing MT1-MMP.
  • To analyze the resulting diffraction pattern for structural insights.

Main Methods:

  • Recombinant expression of human MT1-MMP catalytic domain in E. coli.
  • Protein purification from inclusion bodies using a refolding protocol.
  • Crystallization via the vapour diffusion method.

Main Results:

  • Significant quantities of active MT1-MMP catalytic domain were obtained.
  • Crystals of MT1-MMP were successfully grown.
  • Data analysis and diffraction patterns were generated.

Conclusions:

  • The study successfully established protocols for obtaining active MT1-MMP catalytic domain.
  • Crystallization of MT1-MMP provides a basis for future structural studies.
  • Understanding MT1-MMP structure is crucial for targeting cancer progression.
Keywords:
CrystallizationDiffractionMMP-14MT1-MMPMetalloproteinase

More Related Videos

Detection of Functional Matrix Metalloproteinases by Zymography09:30

Detection of Functional Matrix Metalloproteinases by Zymography

Published on: November 8, 2010

85.1K
Derivatization of Protein Crystals with I3C using Random Microseed Matrix Screening14:04

Derivatization of Protein Crystals with I3C using Random Microseed Matrix Screening

Published on: January 16, 2021

5.0K

Related Concept Videos

Role of Matrix Metalloproteases in Degradation of ECM01:23

Role of Matrix Metalloproteases in Degradation of ECM

Matrix metalloproteases (MMPs) are enzymes involved in the hydrolysis of proteins and glycoproteins of the extracellular matrix. MMPs are essential for the migration and proliferation of cells through the dense matrix network, throughout embryonic development, and throughout morphogenesis. The first MMP activity discovered was a collagenase in a tadpole's tail undergoing metamorphosis. The active collagen deposition and modifications lead to the morphogenesis of tadpoles into the adult...
3.6K
X-ray Diffraction of Biological Samples01:10

X-ray Diffraction of Biological Samples

X-ray diffraction or XRD is an analytical tool that utilizes X-rays to study ordered structures such as crystalline organic and inorganic samples, polycrystalline materials, proteins, carbohydrates, and drugs.
According to Bragg's law, when X-rays strike the sample positioned on a stage, the rays are  scattered by the electron clouds around the sample atoms. The  X-ray diffraction or scattering is caused by constructive interference of the X-ray waves that reflect off the internal...
5.0K