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Crystallization and Preliminary X-Ray Crystallographic Analysis of bHLH Domain of Aryl Hydrocarbon Receptor Nucleus Translocator

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The basic-helix-loop-helix(bHLH) DNA binding domain of Aryl hydrocarbon receptor nucleus translocator (Arnt) was purified and crystallized in glutathione S transferase (GST) fusion form. The tetragonal crystal was grown in ammonium sulfate condition and diffracted up to 2.2 A.

Keywords: CRYSTALLIZATION AND PRELIMINARY X-RAY; DNA binding domain; nucleus translocator

Document Type: Review Article


Affiliations: Department of Life Science, Kwangju Institute of Science and Technology(K-JIST), Kwangju 500-712, KOREA

Publication date: October 1, 2001

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.

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