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

Publication: Research - peer-reviewJournal article – Annual report year: 2004

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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.
Original languageEnglish
JournalActa Crystallographica Section D
Publication date2004
Volume60
Pages472-478
DOIs
StatePublished
CitationsWeb of Science® Times Cited: 5
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