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Related Concept Videos

Iterative Optimization of DNA Duplexes for Crystallization of SeqA-DNA Complexes11:42

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Crystal structure of protein–DNA complexes can provide insight into protein function, mechanism, as well as, the nature of the specific interaction. Here, we report how to optimize the length, sequence and ends of duplex DNA for co-crystallization with Escherichia coli SeqA, a negative regulator of replication...
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Crystal Field Theory
To explain the observed behavior of transition metal complexes (such as colors), a model involving electrostatic interactions between the electrons from the ligands and the electrons in the unhybridized d orbitals of the central metal atom has been developed. This electrostatic model is crystal field theory (CFT). It helps to understand, interpret, and predict the colors, magnetic behavior, and some structures of coordination compounds of transition metals.
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Ionic Crystal Structures

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Ionic crystals consist of two or more different kinds of ions that usually have different sizes. The packing of these ions into a crystal structure is more complex than the packing of metal atoms that are the same size.
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Related Experiment Video

Updated: Jan 20, 2026

Iterative Optimization of DNA Duplexes for Crystallization of SeqA-DNA Complexes
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Iterative Optimization of DNA Duplexes for Crystallization of SeqA-DNA Complexes

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Crystal Structure of FOXC2 in Complex with DNA Target.

Shichang Li1, Lagnajeet Pradhan1, Shayan Ashur1

  • 1Department of Bioengineering, The University of Texas at Dallas, 800 W. Campbell Road, Richardson, Texas 75080, United States.

ACS Omega
|August 29, 2019
PubMed
Summary

Forkhead transcription factor C2 (FOXC2) regulates development and metastasis. Its crystal structure reveals how FOXC2 recognizes DNA, aiding in understanding mutations linked to lymphedema and cancer progression.

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Crystallization and Structural Determination of an Enzyme:Substrate Complex by Serial Crystallography in a Versatile Microfluidic Chip
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Crystal Field Theory - Octahedral Complexes
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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Genetics

Background:

  • Forkhead transcription factor C2 (FOXC2) is vital for vascular and lymphatic development.
  • FOXC2 mutations cause lymphedema-distichiasis syndrome and are implicated in tumor metastasis via epithelial-mesenchymal transition.
  • Understanding FOXC2-DNA interactions is crucial for deciphering its regulatory roles and disease associations.

Purpose of the Study:

  • To determine the crystal structure of the FOXC2 DNA-binding domain in complex with its target DNA.
  • To elucidate the molecular basis of DNA sequence recognition by FOXC2.
  • To provide insights into how mutations affect FOXC2 function.

Main Methods:

  • X-ray crystallography to obtain the FOXC2-DNA complex structure.
  • Computational energy calculations to validate structural findings.

Main Results:

  • The crystal structure reveals the FOXC2 DNA-binding domain complexed with its cognate DNA, specifically the T/CAAAC motif.
  • Helix 3 of FOXC2 is critical for DNA sequence recognition, mediating most DNA-protein interactions.
  • Computational analysis supports the structural observations regarding protein-DNA binding specificity.

Conclusions:

  • The determined structure provides a detailed atomic-level understanding of FOXC2-DNA interactions.
  • This structural information enables prediction of FOXC2 DNA recognition specificity.
  • The findings facilitate the analysis of impaired FOXC2 functions in mutants found in human diseases.