Purification, crystallization and X-ray diffraction analysis of pavine N-methyltransferase from Thalictrum flavum

Ankur Jain; Jörg Ziegler; David K. Liscombe; Peter J. Facchini; Paul A. Tucker; Santosh Panjikar

doi:10.1107/S1744309108033046

Purification, crystallization and X-ray diffraction analysis of pavine N-methyltransferase from Thalictrum flavum

Ankur Jain
, Jörg Ziegler
, David K. Liscombe
, Peter J. Facchini
, Paul A. Tucker
, Santosh Panjikar

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

4 Citations (Scopus)

Abstract

A cDNA from the plant Thalictrum flavum encoding pavine N-methyltransferase, an enzyme belonging to a novel class of S-adenosylmethionine-dependent N-methyltransferases specific for benzylisoquinoline alkaloids, has been heterologously expressed in Escherichia coli. The enzyme was purified using affinity and gel-filtration chromatography and was crystallized in space group P2₁. The structure was solved at 2.0 Å resolution using a xenon derivative and the single isomorphous replacement with anomalous scattering method.

Original language	English
Pages (from-to)	1066-1069
Number of pages	4
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Volume	64
Issue number	11
DOIs	https://doi.org/10.1107/S1744309108033046
Publication status	Published - 2008
Externally published	Yes

Keywords

Pavine N-methyltransferase
Thalictrum flavum

Access to Document

10.1107/S1744309108033046

Cite this

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title = "Purification, crystallization and X-ray diffraction analysis of pavine N-methyltransferase from Thalictrum flavum",

abstract = "A cDNA from the plant Thalictrum flavum encoding pavine N-methyltransferase, an enzyme belonging to a novel class of S-adenosylmethionine-dependent N-methyltransferases specific for benzylisoquinoline alkaloids, has been heterologously expressed in Escherichia coli. The enzyme was purified using affinity and gel-filtration chromatography and was crystallized in space group P21. The structure was solved at 2.0 {\AA} resolution using a xenon derivative and the single isomorphous replacement with anomalous scattering method.",

keywords = "Pavine N-methyltransferase, Thalictrum flavum",

author = "Ankur Jain and J{\"o}rg Ziegler and Liscombe, \{David K.\} and Facchini, \{Peter J.\} and Tucker, \{Paul A.\} and Santosh Panjikar",

year = "2008",

doi = "10.1107/S1744309108033046",

language = "English",

volume = "64",

pages = "1066--1069",

journal = "Acta Crystallographica Section F: Structural Biology and Crystallization Communications",

issn = "1744-3091",

publisher = "International Union of Crystallography (IUCr)",

number = "11",

}

Purification, crystallization and X-ray diffraction analysis of pavine N-methyltransferase from Thalictrum flavum. / Jain, Ankur; Ziegler, Jörg; Liscombe, David K. et al.
In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 64, No. 11, 2008, p. 1066-1069.

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

TY - JOUR

T1 - Purification, crystallization and X-ray diffraction analysis of pavine N-methyltransferase from Thalictrum flavum

AU - Jain, Ankur

AU - Ziegler, Jörg

AU - Liscombe, David K.

AU - Facchini, Peter J.

AU - Tucker, Paul A.

AU - Panjikar, Santosh

PY - 2008

Y1 - 2008

N2 - A cDNA from the plant Thalictrum flavum encoding pavine N-methyltransferase, an enzyme belonging to a novel class of S-adenosylmethionine-dependent N-methyltransferases specific for benzylisoquinoline alkaloids, has been heterologously expressed in Escherichia coli. The enzyme was purified using affinity and gel-filtration chromatography and was crystallized in space group P21. The structure was solved at 2.0 Å resolution using a xenon derivative and the single isomorphous replacement with anomalous scattering method.

AB - A cDNA from the plant Thalictrum flavum encoding pavine N-methyltransferase, an enzyme belonging to a novel class of S-adenosylmethionine-dependent N-methyltransferases specific for benzylisoquinoline alkaloids, has been heterologously expressed in Escherichia coli. The enzyme was purified using affinity and gel-filtration chromatography and was crystallized in space group P21. The structure was solved at 2.0 Å resolution using a xenon derivative and the single isomorphous replacement with anomalous scattering method.

KW - Pavine N-methyltransferase

KW - Thalictrum flavum

UR - https://www.scopus.com/pages/publications/55949116985

U2 - 10.1107/S1744309108033046

DO - 10.1107/S1744309108033046

M3 - Article

C2 - 18997344

AN - SCOPUS:55949116985

SN - 1744-3091

VL - 64

SP - 1066

EP - 1069

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

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

IS - 11

ER -

Purification, crystallization and X-ray diffraction analysis of pavine N-methyltransferase from Thalictrum flavum

Abstract

Keywords

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