Journal
STRUCTURE
Volume 15, Issue 3, Pages 267-273Publisher
CELL PRESS
DOI: 10.1016/j.str.2007.01.011
Keywords
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Funding
- Medical Research Council [G0400717, G9900061] Funding Source: Medline
- Wellcome Trust [081894] Funding Source: Medline
- MRC [G0400717, G9900061] Funding Source: UKRI
- Medical Research Council [G9900061, G0400717] Funding Source: researchfish
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Glycoproteins present special problems for structural genomic analysis because they often require glycosylation in order to fold correctly which then leads to chemical and conformational heterogeneity that often inhibits crystallization. We show that the glycosylation problem can be solved by expressing glycoproteins transiently in mammalian cells in the presence of the N-glycosylation processing inhibitors, kifunensine or swainsonine. This allows the correct folding of the glycoproteins, but leaves them sensitive to enzymes, such as endoglycosidase H, that reduce the N-glycans to single residues, enhancing crystallization. Since the scalability of transient mammalian expression is now comparable to that of bacterial systems, this approach should relieve one of the major bottlenecks in structural genomic analysis.
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