@ARTICLE{Gadd2009151,
author={Gadd, M.S. and Langley, D.B. and Guss, J.M. and Matthews, J.M.},
title={Crystallization and diffraction of an Lhx4-Isl2 complex},
journal={Acta Crystallographica Section F: Structural Biology and Crystallization Communications},
year={2009},
volume={65},
number={2},
pages={151-153},
doi={10.1107/S1744309108043431},
note={cited By 5},
url={https://www.scopus.com/inward/record.uri?eid=2-s2.0-59749083097&doi=10.1107%2fS1744309108043431&partnerID=40&md5=d34848842bad97d5751ef67a8356913b},
affiliation={School of Molecular and Microbial Biosciences, University of Sydney, Australia},
abstract={A stable intramolecular complex comprising the LIM domains of the LIM-homeodomain protein Lhx4 tethered to a peptide region of Isl2 has been engineered, purified and crystallized. The monoclinic crystals belonged to space group P21, with unit-cell parameters a = 46.8, b = 88.7, c = 49.9 Å, β = 111.9°, and diffracted to 2.16 Å resolution. © International Union of Crystallography 2009.},
author_keywords={Isl2;  Lhx4;  Lim domains;  Lim-homeodomain transcription factors},
keywords={homeodomain protein;  insulin gene enhancer binding protein Isl 1;  insulin gene enhancer binding protein Isl-1;  Lhx4 protein, mouse;  nerve protein;  transcription factor, animal;  article;  chemistry;  comparative study;  crystallization;  metabolism;  methodology;  motoneuron;  mouse;  physiology;  protein binding;  protein engineering;  X ray diffraction, Animals;  Crystallization;  Homeodomain Proteins;  Mice;  Motor Neurons;  Nerve Tissue Proteins;  Protein Binding;  Protein Engineering;  Transcription Factors;  X-Ray Diffraction},
correspondence_address1={Matthews, J. M.; School of Molecular and Microbial Biosciences, Australia; email: j.matthews@usyd.edu.au},
issn={17443091},
pubmed_id={19194008},
language={English},
abbrev_source_title={Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun.},
document_type={Article},
source={Scopus},
}

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