Cloning, purification and preliminary X-ray crystallographic analysis of the OmpA-like domain of peptidoglycan-associated lipoprotein fromAcinetobacter baumannii
2012 ◽
Vol 68
(11)
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pp. 1351-1353
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Keyword(s):
X Ray
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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 fromAcinetobacter baumanniiwas overexpressed inEscherichia colistrain BL21 (DE3), purified and crystallized using the vapour-diffusion method. A native crystal diffracted to 1.4 Å resolution and belonged to space groupP61orP65, with unit-cell parametersa=b= 72.58,c= 44.65 Å, a calculated Matthews coefficient of 2.64 Å3 Da−1and one molecule per asymmetric unit.
2014 ◽
Vol 70
(11)
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pp. 1560-1562
2015 ◽
Vol 71
(3)
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pp. 261-265
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2015 ◽
Vol 71
(3)
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pp. 354-357
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2015 ◽
Vol 71
(8)
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pp. 1109-1113
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2016 ◽
Vol 72
(6)
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pp. 480-484
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2014 ◽
Vol 70
(5)
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pp. 600-603
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