Purification, crystallization and preliminary X-ray crystallographic analysis of 23S RNA m2G2445 methyltransferase RlmL from Escherichia coli

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Standard

Purification, crystallization and preliminary X-ray crystallographic analysis of 23S RNA m2G2445 methyltransferase RlmL from Escherichia coli. / Wang, Kai Tuo; Ma, Linglong; Nan, Jie; Su, Xiao Dong; Li, Lanfen.

In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 66, No. 11, 01.11.2010, p. 1484-1486.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Wang, KT, Ma, L, Nan, J, Su, XD & Li, L 2010, 'Purification, crystallization and preliminary X-ray crystallographic analysis of 23S RNA m2G2445 methyltransferase RlmL from Escherichia coli', Acta Crystallographica Section F: Structural Biology and Crystallization Communications, vol. 66, no. 11, pp. 1484-1486. https://doi.org/10.1107/S1744309110035074

APA

Wang, K. T., Ma, L., Nan, J., Su, X. D., & Li, L. (2010). Purification, crystallization and preliminary X-ray crystallographic analysis of 23S RNA m2G2445 methyltransferase RlmL from Escherichia coli. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 66(11), 1484-1486. https://doi.org/10.1107/S1744309110035074

Vancouver

Wang KT, Ma L, Nan J, Su XD, Li L. Purification, crystallization and preliminary X-ray crystallographic analysis of 23S RNA m2G2445 methyltransferase RlmL from Escherichia coli. Acta Crystallographica Section F: Structural Biology and Crystallization Communications. 2010 Nov 1;66(11):1484-1486. https://doi.org/10.1107/S1744309110035074

Author

Wang, Kai Tuo ; Ma, Linglong ; Nan, Jie ; Su, Xiao Dong ; Li, Lanfen. / Purification, crystallization and preliminary X-ray crystallographic analysis of 23S RNA m2G2445 methyltransferase RlmL from Escherichia coli. In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications. 2010 ; Vol. 66, No. 11. pp. 1484-1486.

Bibtex

@article{e3738f8a89f04aaa80ad573ffe29ebe1,
title = "Purification, crystallization and preliminary X-ray crystallographic analysis of 23S RNA m2G2445 methyltransferase RlmL from Escherichia coli",
abstract = "The RlmL (YcbY) protein in Escherichia coli is an rRNA methyltransferase that is specific for m2G2445 modification of 23S RNA. The rlmL gene was cloned into the expression vector pET28a and expressed in the host E. coli strain BL21 (DE3). Recombinant protein with a six-histidine tag was purified by Ni2+-affinity chromatography followed by gel filtration. Crystals were grown using the hanging-drop vapour-diffusion method and a detergent was used as an additive to improve diffraction quality. The final crystals diffracted to 2.2 {\AA} resolution. The crystals belonged to space group P21, with unit-cell parameters a = 73.6, b = 140.8, c = 102.9 {\AA}, β = 102.3°. The crystal has a most probable solvent content of 62.8% with two molecules in the asymmetric unit.",
keywords = "Echerichia coli, RlmL, rRNA methyltransferases",
author = "Wang, {Kai Tuo} and Linglong Ma and Jie Nan and Su, {Xiao Dong} and Lanfen Li",
year = "2010",
month = nov,
day = "1",
doi = "10.1107/S1744309110035074",
language = "English",
volume = "66",
pages = "1484--1486",
journal = "Acta Crystallographica Section F: Structural Biology Communications",
issn = "2053-230X",
publisher = "Wiley",
number = "11",

}

RIS

TY - JOUR

T1 - Purification, crystallization and preliminary X-ray crystallographic analysis of 23S RNA m2G2445 methyltransferase RlmL from Escherichia coli

AU - Wang, Kai Tuo

AU - Ma, Linglong

AU - Nan, Jie

AU - Su, Xiao Dong

AU - Li, Lanfen

PY - 2010/11/1

Y1 - 2010/11/1

N2 - The RlmL (YcbY) protein in Escherichia coli is an rRNA methyltransferase that is specific for m2G2445 modification of 23S RNA. The rlmL gene was cloned into the expression vector pET28a and expressed in the host E. coli strain BL21 (DE3). Recombinant protein with a six-histidine tag was purified by Ni2+-affinity chromatography followed by gel filtration. Crystals were grown using the hanging-drop vapour-diffusion method and a detergent was used as an additive to improve diffraction quality. The final crystals diffracted to 2.2 Å resolution. The crystals belonged to space group P21, with unit-cell parameters a = 73.6, b = 140.8, c = 102.9 Å, β = 102.3°. The crystal has a most probable solvent content of 62.8% with two molecules in the asymmetric unit.

AB - The RlmL (YcbY) protein in Escherichia coli is an rRNA methyltransferase that is specific for m2G2445 modification of 23S RNA. The rlmL gene was cloned into the expression vector pET28a and expressed in the host E. coli strain BL21 (DE3). Recombinant protein with a six-histidine tag was purified by Ni2+-affinity chromatography followed by gel filtration. Crystals were grown using the hanging-drop vapour-diffusion method and a detergent was used as an additive to improve diffraction quality. The final crystals diffracted to 2.2 Å resolution. The crystals belonged to space group P21, with unit-cell parameters a = 73.6, b = 140.8, c = 102.9 Å, β = 102.3°. The crystal has a most probable solvent content of 62.8% with two molecules in the asymmetric unit.

KW - Echerichia coli

KW - RlmL

KW - rRNA methyltransferases

UR - http://www.scopus.com/inward/record.url?scp=78149311116&partnerID=8YFLogxK

U2 - 10.1107/S1744309110035074

DO - 10.1107/S1744309110035074

M3 - Journal article

C2 - 21045301

AN - SCOPUS:78149311116

VL - 66

SP - 1484

EP - 1486

JO - Acta Crystallographica Section F: Structural Biology Communications

JF - Acta Crystallographica Section F: Structural Biology Communications

SN - 2053-230X

IS - 11

ER -

ID: 234874803