Schenk, Gerhard and Carrington, Lyle E. and Hamilton, Susan E. and de Jersey, John and Guddat, Luke W.
Crystallization and preliminary X-ray diffraction
data for a purple acid phosphatase from sweet
Acta Crystallographica Section D Biological Crystallography, 55 (12).
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.
||binuclear metal centre; metalloenzyme; purple acid phosphatase; protein crystallization;
||Science & Engineering > Chemistry
||28 May 2012 13:07
|Journal or Publication Title:
||Acta Crystallographica Section D Biological Crystallography
||International Union of Crystallography
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