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

Ji-Joon Song; Mun-Kyoung Kim; Eunseon Hur; Hyunsung Park; Soo H. Eom

doi:10.2174/0929866013409283

ISSN: 0929-8665
E-ISSN: 1875-5305

Crystallization and Preliminary X-Ray Crystallographic Analysis of bHLH Domain of Aryl Hydrocarbon Receptor Nucleus Translocator
Authors: Ji-Joon Song¹, Mun-Kyoung Kim², Eunseon Hur³, Hyunsung Park⁴ and Soo H. Eom⁵
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¹ Department of Life Science, Kwangju Institute of Science and Technology(K-JIST), Kwangju 500-712, KOREA ² Department of Life Science, Kwangju Institute of Science and Technology(K-JIST), Kwangju 500-712, KOREA ³ Department of Life Science, Kwangju Institute of Science and Technology(K-JIST), Kwangju 500-712, KOREA ⁴ Department of Life Science, Kwangju Institute of Science and Technology(K-JIST), Kwangju 500-712, KOREA ⁵ Department of Life Science, Kwangju Institute of Science and Technology(K-JIST), Kwangju 500-712, KOREA
Source: Protein and Peptide Letters, Volume 8, Issue 5, Oct 2001, p. 419 - 422
DOI: https://doi.org/10.2174/0929866013409283
- Available online: 01 Oct 2001

Abstract

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.

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2001-10-01

2025-09-01

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Article Type: Review Article

Keyword(s): CRYSTALLIZATION AND PRELIMINARY X-RAY; DNA binding domain; nucleus translocator

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

Abstract

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