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.
Keywords: CRYSTALLIZATION AND PRELIMINARY X-RAY, DNA binding domain, nucleus translocator
Protein & Peptide Letters
Title: Crystallization and Preliminary X-Ray Crystallographic Analysis of bHLH Domain of Aryl Hydrocarbon Receptor Nucleus Translocator
Volume: 8 Issue: 5
Author(s): Ji-Joon Song, Mun-Kyoung Kim, Eunseon Hur, Hyunsung Park and Soo Hyun Eom
Affiliation:
Keywords: CRYSTALLIZATION AND PRELIMINARY X-RAY, DNA binding domain, nucleus translocator
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.
Export Options
About this article
Cite this article as:
Song Ji-Joon, Kim Mun-Kyoung, Hur Eunseon, Park Hyunsung and Eom Hyun Soo, Crystallization and Preliminary X-Ray Crystallographic Analysis of bHLH Domain of Aryl Hydrocarbon Receptor Nucleus Translocator, Protein & Peptide Letters 2001; 8 (5) . https://dx.doi.org/10.2174/0929866013409283
DOI https://dx.doi.org/10.2174/0929866013409283 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
- Author Guidelines
- Graphical Abstracts
- Fabricating and Stating False Information
- Research Misconduct
- Post Publication Discussions and Corrections
- Publishing Ethics and Rectitude
- Increase Visibility of Your Article
- Archiving Policies
- Peer Review Workflow
- Order Your Article Before Print
- Promote Your Article
- Manuscript Transfer Facility
- Editorial Policies
- Allegations from Whistleblowers