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dc.contributor.authorJohnson, Steven
dc.contributor.authorRoversi, Pietro
dc.contributor.authorEspina, Marianela
dc.contributor.authorDeane, Janet E.
dc.contributor.authorBirket, Susan
dc.contributor.authorPicking, William D.
dc.contributor.authorPicking, Wendy Lynn
dc.contributor.authorLea, Susan M.
dc.date.accessioned2016-07-21T18:07:05Z
dc.date.available2016-07-21T18:07:05Z
dc.date.issued2006-08-11
dc.identifier.citationJohnson, S., Roversi, P., Espina, M., Deane, J. E., Birket, S., Picking, W. D., … Lea, S. M. (2006). Expression, limited proteolysis and preliminary crystallographic analysis of IpaD, a component of the Shigella flexneri type III secretion system. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 62(Pt 9), 865–868. http://doi.org/10.1107/S1744309106027047en_US
dc.identifier.urihttp://hdl.handle.net/1808/21169
dc.description.abstractaD, the putative needle-tip protein of the Shigella flexneri type III secretion system, has been overexpressed and purified. Crystals were grown of the native protein in space group P212121, with unit-cell parameters a = 55.9, b = 100.7, c = 112.0 Å, and data were collected to 2.9 Å resolution. Analysis of the native Patterson map revealed a peak at 50% of the origin on the Harker section v = 0.5, suggesting twofold non-crystallographic symmetry parallel to the b crystallographic axis. As attempts to derivatize or grow selenomethionine-labelled protein crystals failed, in-drop proteolysis was used to produce new crystal forms. A trace amount of subtilisin Carlsberg was added to IpaD before sparse-matrix screening, resulting in the production of several new crystal forms. This approach produced SeMet-labelled crystals and diffraction data were collected to 3.2 Å resolution. The SeMet crystals belong to space group C2, with unit-cell parameters a = 139.4, b = 45.0, c = 99.5 Å, β = 107.9°. An anomalous difference Patterson map revealed peaks on the Harker section v = 0, while the self-rotation function indicates the presence of a twofold noncrystallographic symmetry axis, which is consistent with two molecules per asymmetric unit.en_US
dc.publisherInternational Union of Crystallographyen_US
dc.rightsCopyright © International Union of Crystallography 2006. This is an open-access article distributed under the terms described at http://journals.iucr.org/services/termsofuse.html.en_US
dc.subjectIpaDen_US
dc.subjectType III secretionen_US
dc.subjectShigella flexnerien_US
dc.titleExpression, limited proteolysis and preliminary crystallographic analysis of IpaD, a component of the Shigella flexneri type III secretion systemen_US
dc.typeArticleen_US
kusw.kuauthorPicking, Wendy Lynn
kusw.kuauthorEspina, Marianela
kusw.kuauthorBirket, Susan
kusw.kuauthorPicking, William D.
kusw.kudepartmentPharmaceutical Chemistryen_US
dc.identifier.doi10.1107/S1744309106027047en_US
dc.identifier.orcidhttps://orcid.org/0000-0001-7998-0643
kusw.oaversionScholarly/refereed, publisher versionen_US
kusw.oapolicyThis item does not meet KU Open Access policy criteria.en_US
dc.rights.accessrightsopenAccess


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