DNA-Directed Protein Packing within Single Crystals.

Chem

Department of Chemistry, Northwestern University, 2145 Sheridan Road, Evanston, IL 60208, USA.

Published: April 2020

AI Article Synopsis

  • Researchers studied how specifically designed DNA interactions affect the arrangement of mutant green fluorescent proteins (mGFPs) in crystals.
  • The experiments revealed that DNA sequence and attachment points significantly influence crystal formation and protein packing, with complementary DNA leading to consistent packing parameters.
  • This study highlights the potential of engineered DNA to enhance protein crystal growth and organization, which is crucial for advancing protein crystallography techniques.

Article Abstract

Designed DNA-DNA interactions are investigated for their ability to modulate protein packing within single crystals of mutant green fluorescent proteins (mGFPs) functionalized with a single DNA strand (mGFP-DNA). We probe the effects of DNA sequence, length, and protein-attachment position on the formation and protein packing of mGFP-DNA crystals. Notably, when complementary mGFP-DNA conjugates are introduced to one another, crystals form with nearly identical packing parameters, regardless of sequence if the number of bases is equivalent. DNA complementarity is essential, because experiments with non-complementary sequences produce crystals with different protein arrangements. Importantly, the DNA length and its position of attachment on the protein markedly influence the formation of and protein packing within single crystals. This work shows how designed DNA interactions can be used to influence the growth and packing in X-ray diffraction quality protein single crystals and is thus an important step forward in protein crystal engineering.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7946157PMC
http://dx.doi.org/10.1016/j.chempr.2020.03.002DOI Listing

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