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Crystallization and preliminary X-ray diffraction data for a purple acid phosphatase from sweet potato
Schenk, Gerhard; Carrington, Lyle E.; Hamilton, Susan E.; de Jersey, John; Guddat, Luke W.
Purple acid phosphatase from sweet potato is a homodimer of 110 kDa. Two forms of the enzyme have been characterized. One contains an Fe±Zn centre similar to that previously reported for red kidney bean purple acid phosphatase. Another isoform, the subject of this work, is the ®rst con®rmed example of an Fe±Mn-containing enzyme. Crystals of this protein have been grown from PEG 6000. They have unit-cell parameters a = b = 118.4, c = 287.4 A Ê and have the symmetry of space group P6522, with one dimer per asymmetric unit. Diffraction data collected using a conventional X-ray source from a cryocooled crystal extend to 2.90 A Ê resolution. The three-dimensional structure of the enzyme will provide insight into the coordination of this novel binuclear metal centre.
Keyword(s): Chemistry; binuclear metal centre; metalloenzyme; purple acid phosphatase; protein crystallization
Publication Date:
1999
Type: Journal article
Peer-Reviewed: Yes
Institution: Maynooth University
Citation(s): Schenk, Gerhard and Carrington, Lyle E. and Hamilton, Susan E. and de Jersey, John and Guddat, Luke W. (1999) Crystallization and preliminary X-ray diffraction data for a purple acid phosphatase from sweet potato. Acta Crystallographica Section D Biological Crystallography, 55 (12). pp. 2051-2052. ISSN 0907-4449
Publisher(s): International Union of Crystallography
File Format(s): application/pdf
Related Link(s): https://mural.maynoothuniversity.ie/3686/1/GS_Crystallization.pdf
First Indexed: 2020-01-31 06:29:22 Last Updated: 2021-07-31 06:48:01