Journal
STRUCTURE
Volume 15, Issue 7, Pages 773-780Publisher
CELL PRESS
DOI: 10.1016/j.str.2007.05.006
Keywords
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Funding
- NCI NIH HHS [R01 CA077373-09, R01 CA077373, CA077373] Funding Source: Medline
- NIGMS NIH HHS [R01 GM071747-03, GM071747, R01 GM071747] Funding Source: Medline
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Structural studies of macromolecular complexes have produced extraordinary insights into a wide variety of biological processes. Unfortunately, as structural biologists pursue larger and more challenging assemblies, weakly stable and/or nonspecific interactions can become significant roadblocks to structure determination. We have developed a rapid and effective pool-based screen, termed FASTDXL (focused array screening technique for disulfide X-linking), to produce and identify disulfide-stabilized protein-nucleic acid assemblies. A significant strength of FASTDXL is that it can take advantage of prior structural knowledge about molecular interactions, but does not necessarily rely upon it. A detailed application of the approach to the difficult problem of trapping a bacterial primase-ssDNA complex is described, validating the method as a route toward obtaining diffracting crystals suitable for structure determination.
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