Crystal packing in two pH-dependent crystal forms of rhamnogalacturonan acetylesterase

Authors: Mølgaard, Anne; Larsen, Sine

Source: Acta Crystallographica Section D, Volume 60, Number 3, March 2004 , pp. 472-478(7)

Publisher: Blackwell Publishing

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Abstract:

The glycoprotein rhamnogalacturonan acetylesterase from Aspergillus aculeatus has been crystallized in two crystal forms, an orthorhombic and a trigonal crystal form. In the orthorhombic crystal form, the covalently bound carbohydrate at one of the two N-glycosylation sites is involved in crystal contacts. The orthorhombic crystal form was obtained at pH 5.0 and the trigonal crystal form at pH 4.5. In one case, the two crystal forms were found in the same drop at pH 4.7. The differences in crystal packing in the two crystal forms can be explained by the pH-dependent variation in the protonation state of the glutamic acid residues on the protein surface.

Keywords: rhamnogalacturonan acetylesterase; crystal packing; protonation

Document Type: Research article

DOI: 10.1107/S0907444903029767

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