Document Type
Article
Publication Date
9-1-2008
Publication Title
Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Abstract
Crystals of the catalytic subunit of Methanococcus jannaschii aspartate transcarbamoylase in an orthorhombic crystal form contain four crystallographically independent trimers which associate in pairs to form stable staggered complexes that are similar to each other and to a previously determined monoclinic C2 form. Each subunit has a sulfate in the central channel. The catalytic subunits in these complexes show flexibility, with the elbow angles of the monomers differing by up to 7.4 degrees between crystal forms. Moreover, there is also flexibility in the relative orientation of the trimers around their threefold axis in the complexes, with a difference of 4 degrees between crystal forms.
Repository Citation
Vitali, Jacqueline and Colaneri, Michael J., "Structure of the Catalytic Trimer of Methanococcus Jannaschii Aspartate Transcarbamoylase in an Orthorhombic Crystal Form" (2008). Physics Faculty Publications. 112.
https://engagedscholarship.csuohio.edu/sciphysics_facpub/112
Original Citation
Vitali, Jacqueline and Michael J. Colaneri. "Structure of the Catalytic Trimer of Methanococcus Jannaschii Aspartate Transcarbamoylase in an Orthorhombic Crystal Form." Acta Crystallographica Section F: Structural Biology and Crystallization Communications 64 (2008): 776-780.
DOI
10.1107/S1744309108025359
Version
Publisher's PDF
Publisher's Statement
©2008 International Union of Crystallography
Volume
64
Comments
This work was supported in part by startup funds from Cleveland State University (JV) and grants GM071512 (JV) and GM008180 (MJC) from the National Institutes of Health.