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

doi:10.1107/S2053230X13034857

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

Weizmann Institute of Science

Research output: Contribution to journal › Article › peer-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 language	English GB
Pages (from-to)	232-235
Number of pages	4
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Volume	70
Issue number	2
DOIs	https://doi.org/10.1107/S2053230X13034857
State	Published - Feb 2014

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Genetics
Condensed Matter Physics

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10.1107/S2053230X13034857

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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 and Crystallization Communications, 70(2), 232-235. https://doi.org/10.1107/S2053230X13034857

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

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 {\AA} resolution at 100 K. The crystals belonged to space group P43212, with unit-cell parameters a = 62.99, c = 122.60 {\AA}. The crystal contained one molecule per asymmetric unit, with a Matthews coefficient (V M) of 2.90 {\AA}3 Da-1; the solvent content is estimated to be 57.6\%.",

author = "H Ogata and E Decaneto and Moran Grossman and M Havenith and Irit Sagi and W Lubitz and M Knipp",

note = "Cluster of Excellence RESOLV [EXC 1069]; Deutsche Forschungsgemeinschaft; Max Planck Society We are grateful for the technical assistance of Inge Heise, Norbert Dickmann and Yvonne Brandenburger (MPI for Chemical Energy Conversion, Mulheim, Germany). We thank the staff of beamline BL14.2 at BESSY II (Helmholtz-Zentrum Berlin, Germany) for their assistance during data collection. This work was supported by the Cluster of Excellence RESOLV (EXC 1069) funded by the Deutsche Forschungsgemeinschaft. Financial support was also obtained from the Max Planck Society.",

year = "2014",

month = feb,

doi = "10.1107/S2053230X13034857",

language = "الإنجليزيّة",

volume = "70",

pages = "232--235",

number = "2",

}

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 and Crystallization Communications, vol. 70, no. 2, pp. 232-235. https://doi.org/10.1107/S2053230X13034857

Crystallization and preliminary X-ray crystallographic analysis of the catalytic domain of membrane type 1 matrix metalloproteinase. / Ogata, H; Decaneto, E; Grossman, Moran et al.
In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 70, No. 2, 02.2014, p. 232-235.

Research output: Contribution to journal › Article › peer-review

TY - JOUR

T1 - Crystallization and preliminary X-ray crystallographic analysis of the catalytic domain of membrane type 1 matrix metalloproteinase

AU - Ogata, H

AU - Decaneto, E

AU - Grossman, Moran

AU - Havenith, M

AU - Sagi, Irit

AU - Lubitz, W

AU - Knipp, M

N1 - Cluster of Excellence RESOLV [EXC 1069]; Deutsche Forschungsgemeinschaft; Max Planck Society We are grateful for the technical assistance of Inge Heise, Norbert Dickmann and Yvonne Brandenburger (MPI for Chemical Energy Conversion, Mulheim, Germany). We thank the staff of beamline BL14.2 at BESSY II (Helmholtz-Zentrum Berlin, Germany) for their assistance during data collection. This work was supported by the Cluster of Excellence RESOLV (EXC 1069) funded by the Deutsche Forschungsgemeinschaft. Financial support was also obtained from the Max Planck Society.

PY - 2014/2

Y1 - 2014/2

N2 - 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%.

AB - 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%.

UR - https://www.scopus.com/pages/publications/84905446753

U2 - 10.1107/S2053230X13034857

DO - 10.1107/S2053230X13034857

M3 - مقالة

VL - 70

SP - 232

EP - 235

JO - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

JF - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

IS - 2

ER -

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

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