Protein glycosylation, sweet to crystal growth?

Jeroen R. Mesters*, Rolf Hilgenfeld

*Corresponding author for this work
5 Citations (Scopus)


In protein crystallization, post-translational modifications are often considered an annoyance. They are expected to introduce microheterogeneity into the protein and, in addition, in the case of the larger chemical modifications such as glycosylation, to increase surface entropy. On the one hand, these phenomena are said to be bad for crystal growth. On the other hand, many of these modifications are vital for proper folding and functioning of proteins. Over the past few years, we successfully crystallized several different glycoproteins, obtained by heterologous expression or directly isolated from their natural source. The crystallization of these proteins turned out to be fairly straightforward, and moreover, the carbohydrates were frequently found to be involved in forming (critical) intermolecular contacts. Opposite widespread opinions, an unbiased approach in crystallizing glycoproteins should prevail initially. Finally, several methodologies are listed that could be tried as a last resort.

Original languageEnglish
JournalCrystal Growth and Design
Issue number11
Pages (from-to)2251-2253
Number of pages3
Publication statusPublished - 01.11.2007

Research Areas and Centers

  • Academic Focus: Center for Infection and Inflammation Research (ZIEL)


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