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Updated: Jun 8, 2026

Production, Crystallization, and Structure Determination of the IKK-binding Domain of NEMO

Production, Crystallization, and Structure Determination of the IKK-binding Domain of NEMO

Published on: December 28, 2019

NMR in a crystallography-based high-throughput protein structure-determination environment.

Kurt Wüthrich¹

¹Department of Molecular Biology and Skaggs Institute of Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037, USA. wuthrich@scripps.edu

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications

|October 15, 2010

Summary

This study introduces how combining protein crystallography and Nuclear Magnetic Resonance (NMR) spectroscopy aids structural biology. It highlights the Joint Center for Structural Genomics

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Area of Science:

Structural Biology
Biophysics
Molecular Biology

Background:

The Joint Center for Structural Genomics (JCSG) has determined numerous protein structures using both X-ray crystallography and Nuclear Magnetic Resonance (NMR) spectroscopy.
Comparing these structures provides insights into protein dynamics and conformational flexibility.

Purpose of the Study:

To introduce three papers that compare protein crystal and NMR solution structures.
To discuss the JCSG's strategy for integrating these two structural biology techniques.
To explore the concept and applications of 'reference crystal structures'.

Main Methods:

Comparison of corresponding protein crystal structures.
Comparison of corresponding NMR solution structures.

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Production, Crystallization, and Structure Determination of the IKK-binding Domain of NEMO

Production, Crystallization, and Structure Determination of the IKK-binding Domain of NEMO

Published on: December 28, 2019

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Analysis of the JCSG's combined use strategy for structural determination.

Main Results:

The introduction sets the stage for detailed comparisons presented in subsequent papers.
The JCSG's integrated approach leverages the strengths of both crystallography and NMR.
The concept of 'reference crystal structures' is proposed for further investigation.

Conclusions:

The combined use of crystallography and NMR offers a powerful approach to structural biology.
Reference crystal structures have potential applications in understanding protein structure-function relationships.
This work facilitates a deeper understanding of protein structural ensembles.