Refolding, crystallization and preliminary X-ray crystallographic study of the whole extracellular regions of nectins
2011

Study of Nectins and Their Crystallization

publication Evidence: moderate

Author Information

Author(s): Narita Hirotaka, Nakagawa Atsushi, Yamamoto Yasunori, Sakisaka Toshiaki, Takai Yoshimi, Suzuki Mamoru

Primary Institution: Osaka University

Hypothesis

How do nectin-family members form cis-interactions and trans-interactions?

Conclusion

The study successfully refolded and crystallized the extracellular regions of nectin-1 and nectin-2, providing insights into their structural properties.

Supporting Evidence

  • The whole extracellular regions of nectin-1 and nectin-2 were expressed in E. coli as inclusion bodies.
  • Refolded proteins were purified using three chromatographic steps.
  • Nectin-1-EC crystals belonged to space group P213 and nectin-2-EC crystals belonged to space groups P6122 or P6522.

Takeaway

Scientists figured out how to make and study special proteins called nectins, which help cells stick together. They made these proteins into crystals to see their structure better.

Methodology

The extracellular regions of nectin-1 and nectin-2 were expressed in E. coli, refolded, purified, and crystallized using the hanging-drop vapour-diffusion method.

Limitations

The study did not successfully obtain crystals of nectin-1-EC without a C-terminal 6Ă—His tag.

Digital Object Identifier (DOI)

10.1107/S174430911100337X

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