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Crystallization and preliminary X-ray analysis of 4-coumarate:CoA ligase from Arabidopsis thaliana.


ABSTRACT: 4-Coumarate:CoA ligase 2 (4CL2) from Arabidopsis thaliana catalyzes the ATP-dependent formation of the 4-coumaroyl-CoA thioester through the formation of 4-coumarate-AMP. Recombinant 4CL2 protein was expressed in Escherichia coli and crystallized by the sitting-drop vapour-diffusion method. The crystals belonged to space group P2(1), with unit-cell parameters a=91.6, b=55.5, c=124.4?Å, ?=?=90.0, ?=111.1°.

SUBMITTER: Morita H 

PROVIDER: S-EPMC3053174 | biostudies-literature | 2011 Mar

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray analysis of 4-coumarate:CoA ligase from Arabidopsis thaliana.

Morita Hiroyuki H   Mori Takahiro T   Wanibuchi Kiyofumi K   Kato Ryohei R   Sugio Shigetoshi S   Abe Ikuro I  

Acta crystallographica. Section F, Structural biology and crystallization communications 20110225 Pt 3


4-Coumarate:CoA ligase 2 (4CL2) from Arabidopsis thaliana catalyzes the ATP-dependent formation of the 4-coumaroyl-CoA thioester through the formation of 4-coumarate-AMP. Recombinant 4CL2 protein was expressed in Escherichia coli and crystallized by the sitting-drop vapour-diffusion method. The crystals belonged to space group P2(1), with unit-cell parameters a=91.6, b=55.5, c=124.4 Å, α=γ=90.0, β=111.1°. ...[more]

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