Preliminary X-ray analysis of twinned crystals of sarcosine dimethylglycine methyltransferase from Halorhodospira halochoris

J.P. Kallio, J. Jänis, Antti Nyyssölä, N. Hakulinen, J. Rouvinen (Corresponding Author)

Research output: Contribution to journalArticleScientificpeer-review

1 Citation (Scopus)

Abstract

Sarcosine dimethylglycine methyltransferase (EC 2.1.1.157) is an enzyme from the extremely halophilic anaerobic bacterium Halorhodospira halochoris. This enzyme catalyzes the twofold methylation of sarcosine to betaine, with S-­adenosylmethionine (AdoMet) as the methyl-group donor. This study presents the crystallization and preliminary X-ray analysis of recombinant sarcosine dimethylglycine methyltransferase produced in Escherichia coli. Mass spectroscopy was used to determine the purity and homogeneity of the enzyme material. Two different crystal forms, which initially appeared to be hexagonal and tetragonal, were obtained. However, on analyzing the diffraction data it was discovered that both crystal forms were pseudo-merohedrally twinned. The true crystal systems were monoclinic and orthorhombic. The monoclinic crystal diffracted to a maximum of 2.15 Å resolution and the orthorhombic crystal diffracted to 1.8 Å resolution.
Original languageEnglish
Pages (from-to)805-808
Number of pages4
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume65
Issue number8
DOIs
Publication statusPublished - 2009
MoE publication typeA1 Journal article-refereed

Fingerprint

Sarcosine
X ray analysis
Methyltransferases
X-Rays
Crystals
Enzymes
enzymes
crystals
S-Adenosylmethionine
Betaine
x rays
Anaerobic Bacteria
Crystallization
Methylation
Mass Spectrometry
betaines
methylation
Escherichia coli
Escherichia
bacteria

Keywords

  • Halorhodospira halochoris
  • Sarcosine dimethylglycine methyltransferase
  • Twinning

Cite this

@article{b8291ad970964eedb2703835839d7a64,
title = "Preliminary X-ray analysis of twinned crystals of sarcosine dimethylglycine methyltransferase from Halorhodospira halochoris",
abstract = "Sarcosine dimethylglycine methyltransferase (EC 2.1.1.157) is an enzyme from the extremely halophilic anaerobic bacterium Halorhodospira halochoris. This enzyme catalyzes the twofold methylation of sarcosine to betaine, with S-­adenosylmethionine (AdoMet) as the methyl-group donor. This study presents the crystallization and preliminary X-ray analysis of recombinant sarcosine dimethylglycine methyltransferase produced in Escherichia coli. Mass spectroscopy was used to determine the purity and homogeneity of the enzyme material. Two different crystal forms, which initially appeared to be hexagonal and tetragonal, were obtained. However, on analyzing the diffraction data it was discovered that both crystal forms were pseudo-merohedrally twinned. The true crystal systems were monoclinic and orthorhombic. The monoclinic crystal diffracted to a maximum of 2.15 {\AA} resolution and the orthorhombic crystal diffracted to 1.8 {\AA} resolution.",
keywords = "Halorhodospira halochoris, Sarcosine dimethylglycine methyltransferase, Twinning",
author = "J.P. Kallio and J. J{\"a}nis and Antti Nyyss{\"o}l{\"a} and N. Hakulinen and J. Rouvinen",
year = "2009",
doi = "10.1107/S1744309109026232",
language = "English",
volume = "65",
pages = "805--808",
journal = "Acta Crystallographica Section F: Structural Biology Communications",
issn = "2053-230X",
publisher = "International Union of Crystallography",
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Preliminary X-ray analysis of twinned crystals of sarcosine dimethylglycine methyltransferase from Halorhodospira halochoris. / Kallio, J.P.; Jänis, J.; Nyyssölä, Antti; Hakulinen, N.; Rouvinen, J. (Corresponding Author).

In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 65, No. 8, 2009, p. 805-808.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Preliminary X-ray analysis of twinned crystals of sarcosine dimethylglycine methyltransferase from Halorhodospira halochoris

AU - Kallio, J.P.

AU - Jänis, J.

AU - Nyyssölä, Antti

AU - Hakulinen, N.

AU - Rouvinen, J.

PY - 2009

Y1 - 2009

N2 - Sarcosine dimethylglycine methyltransferase (EC 2.1.1.157) is an enzyme from the extremely halophilic anaerobic bacterium Halorhodospira halochoris. This enzyme catalyzes the twofold methylation of sarcosine to betaine, with S-­adenosylmethionine (AdoMet) as the methyl-group donor. This study presents the crystallization and preliminary X-ray analysis of recombinant sarcosine dimethylglycine methyltransferase produced in Escherichia coli. Mass spectroscopy was used to determine the purity and homogeneity of the enzyme material. Two different crystal forms, which initially appeared to be hexagonal and tetragonal, were obtained. However, on analyzing the diffraction data it was discovered that both crystal forms were pseudo-merohedrally twinned. The true crystal systems were monoclinic and orthorhombic. The monoclinic crystal diffracted to a maximum of 2.15 Å resolution and the orthorhombic crystal diffracted to 1.8 Å resolution.

AB - Sarcosine dimethylglycine methyltransferase (EC 2.1.1.157) is an enzyme from the extremely halophilic anaerobic bacterium Halorhodospira halochoris. This enzyme catalyzes the twofold methylation of sarcosine to betaine, with S-­adenosylmethionine (AdoMet) as the methyl-group donor. This study presents the crystallization and preliminary X-ray analysis of recombinant sarcosine dimethylglycine methyltransferase produced in Escherichia coli. Mass spectroscopy was used to determine the purity and homogeneity of the enzyme material. Two different crystal forms, which initially appeared to be hexagonal and tetragonal, were obtained. However, on analyzing the diffraction data it was discovered that both crystal forms were pseudo-merohedrally twinned. The true crystal systems were monoclinic and orthorhombic. The monoclinic crystal diffracted to a maximum of 2.15 Å resolution and the orthorhombic crystal diffracted to 1.8 Å resolution.

KW - Halorhodospira halochoris

KW - Sarcosine dimethylglycine methyltransferase

KW - Twinning

U2 - 10.1107/S1744309109026232

DO - 10.1107/S1744309109026232

M3 - Article

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SP - 805

EP - 808

JO - Acta Crystallographica Section F: Structural Biology Communications

JF - Acta Crystallographica Section F: Structural Biology Communications

SN - 2053-230X

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