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Overexpression, purification, crystallization and preliminary X-ray crystallographic analysis of the periplasmic domain of outer membrane protein A from Acinetobacter baumannii

Authors
Park, Jeong SoonLee, Woo CheolChoi, SaehaeYeo, Kwon JooSong, Jung HyunHan, Young-HyunLee, Je ChulKim, Seung IlJeon, Young HoCheong, ChaejoonKim, Hye-Yeon
Issue Date
12월-2011
Publisher
INT UNION CRYSTALLOGRAPHY
Keywords
OmpA; Acinetobacter baumannii; peptidoglycan
Citation
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, v.67, pp.1531 - 1533
Indexed
SCOPUS
Journal Title
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
Volume
67
Start Page
1531
End Page
1533
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/111032
DOI
10.1107/S1744309111038401
ISSN
2053-230X
Abstract
Outer membrane protein A from Acinetobacter baumannii (AbOmpA) is a major outer membrane protein and a key player in the bacterial pathogenesis that induces host cell death. AbOmpA is presumed to consist of an N-terminal beta-barrel transmembrane domain and a C-terminal periplasmic OmpA-like domain. In this study, the recombinant C-terminal periplasmic domain of AbOmpA was overexpressed in Escherichia coli, purified and crystallized using the vapour-diffusion method. A native diffraction data set was collected to a resolution of 2.0 angstrom using synchrotron radiation. The space group of the crystal was P21, with unit-cell parameters a = 58.24, b = 98.59, c = 97.96 angstrom, beta = 105.92 degrees. The native crystal contained seven or eight molecules per asymmetric unit and had a calculated Matthews coefficient of 2.93 or 2.56 angstrom 3 Da-1.
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약학대학 (약학과)
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