Cloning, purification and preliminary X-ray crystallographic analysis of the OmpA-like domain of peptidoglycan-associated lipoprotein from Acinetobacter baumannii

Jung Hyun Song; Woo Cheol Lee; Jeong Soon Park; Seung Il Kim; Je Chul Lee; Chaejoon Cheong; Hye Yeon Kim

doi:10.1107/S1744309112038924

Cloning, purification and preliminary X-ray crystallographic analysis of the OmpA-like domain of peptidoglycan-associated lipoprotein from Acinetobacter baumannii

Jung Hyun Song, Woo Cheol Lee, Jeong Soon Park, Seung Il Kim, Je Chul Lee, Chaejoon Cheong, Hye Yeon Kim

Department of Medicine

Korea Basic Science Institute

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

2 Scopus citations

Abstract

Peptidoglycan-associated lipoprotein (Pal) is one component of the Tol-Pal system that is involved in maintaining the integrity and stability of the outer membrane. The C-terminal OmpA-like domain of Pal interacts noncovalently with peptidoglycan. In this study, the OmpA-like domain of Pal from Acinetobacter baumannii was overexpressed in Escherichia coli strain BL21 (DE3), purified and crystallized using the vapour-diffusion method. A native crystal diffracted to 1.4 Å resolution and belonged to space group P61 or P65, with unit-cell parameters a = b = 72.58, c = 44.65 Å, a calculated Matthews coefficient of 2.64 Å³ Da^-1 and one molecule per asymmetric unit.

Original language	English
Pages (from-to)	1351-1353
Number of pages	3
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Volume	68
Issue number	11
DOIs	https://doi.org/10.1107/S1744309112038924
State	Published - Nov 2012

Keywords

OmpA-like domains
peptidoglycan-associated lipoprotein

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10.1107/S1744309112038924

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Song, J. H., Lee, W. C., Park, J. S., Kim, S. I., Lee, J. C., Cheong, C., & Kim, H. Y. (2012). Cloning, purification and preliminary X-ray crystallographic analysis of the OmpA-like domain of peptidoglycan-associated lipoprotein from Acinetobacter baumannii. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 68(11), 1351-1353. https://doi.org/10.1107/S1744309112038924

@article{e91aef5dae804fa8976bc967adf8867c,

title = "Cloning, purification and preliminary X-ray crystallographic analysis of the OmpA-like domain of peptidoglycan-associated lipoprotein from Acinetobacter baumannii",

abstract = "Peptidoglycan-associated lipoprotein (Pal) is one component of the Tol-Pal system that is involved in maintaining the integrity and stability of the outer membrane. The C-terminal OmpA-like domain of Pal interacts noncovalently with peptidoglycan. In this study, the OmpA-like domain of Pal from Acinetobacter baumannii was overexpressed in Escherichia coli strain BL21 (DE3), purified and crystallized using the vapour-diffusion method. A native crystal diffracted to 1.4 {\AA} resolution and belonged to space group P61 or P65, with unit-cell parameters a = b = 72.58, c = 44.65 {\AA}, a calculated Matthews coefficient of 2.64 {\AA}3 Da-1 and one molecule per asymmetric unit.",

keywords = "OmpA-like domains, peptidoglycan-associated lipoprotein",

author = "Song, {Jung Hyun} and Lee, {Woo Cheol} and Park, {Jeong Soon} and Kim, {Seung Il} and Lee, {Je Chul} and Chaejoon Cheong and Kim, {Hye Yeon}",

year = "2012",

month = nov,

doi = "10.1107/S1744309112038924",

language = "English",

volume = "68",

pages = "1351--1353",

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

issn = "1744-3091",

publisher = "John Wiley and Sons Ltd",

number = "11",

}

Song, JH, Lee, WC, Park, JS, Kim, SI, Lee, JC, Cheong, C & Kim, HY 2012, 'Cloning, purification and preliminary X-ray crystallographic analysis of the OmpA-like domain of peptidoglycan-associated lipoprotein from Acinetobacter baumannii', Acta Crystallographica Section F: Structural Biology and Crystallization Communications, vol. 68, no. 11, pp. 1351-1353. https://doi.org/10.1107/S1744309112038924

Cloning, purification and preliminary X-ray crystallographic analysis of the OmpA-like domain of peptidoglycan-associated lipoprotein from Acinetobacter baumannii. / Song, Jung Hyun; Lee, Woo Cheol; Park, Jeong Soon et al.
In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 68, No. 11, 11.2012, p. 1351-1353.

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

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T1 - Cloning, purification and preliminary X-ray crystallographic analysis of the OmpA-like domain of peptidoglycan-associated lipoprotein from Acinetobacter baumannii

AU - Song, Jung Hyun

AU - Lee, Woo Cheol

AU - Park, Jeong Soon

AU - Kim, Seung Il

AU - Lee, Je Chul

AU - Cheong, Chaejoon

AU - Kim, Hye Yeon

PY - 2012/11

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N2 - Peptidoglycan-associated lipoprotein (Pal) is one component of the Tol-Pal system that is involved in maintaining the integrity and stability of the outer membrane. The C-terminal OmpA-like domain of Pal interacts noncovalently with peptidoglycan. In this study, the OmpA-like domain of Pal from Acinetobacter baumannii was overexpressed in Escherichia coli strain BL21 (DE3), purified and crystallized using the vapour-diffusion method. A native crystal diffracted to 1.4 Å resolution and belonged to space group P61 or P65, with unit-cell parameters a = b = 72.58, c = 44.65 Å, a calculated Matthews coefficient of 2.64 Å3 Da-1 and one molecule per asymmetric unit.

AB - Peptidoglycan-associated lipoprotein (Pal) is one component of the Tol-Pal system that is involved in maintaining the integrity and stability of the outer membrane. The C-terminal OmpA-like domain of Pal interacts noncovalently with peptidoglycan. In this study, the OmpA-like domain of Pal from Acinetobacter baumannii was overexpressed in Escherichia coli strain BL21 (DE3), purified and crystallized using the vapour-diffusion method. A native crystal diffracted to 1.4 Å resolution and belonged to space group P61 or P65, with unit-cell parameters a = b = 72.58, c = 44.65 Å, a calculated Matthews coefficient of 2.64 Å3 Da-1 and one molecule per asymmetric unit.

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

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Cloning, purification and preliminary X-ray crystallographic analysis of the OmpA-like domain of peptidoglycan-associated lipoprotein from Acinetobacter baumannii

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