Crystallization of an Lhx3–Isl1 complex
Journal Article
·
· Acta Crystallographica. Section F
- School of Molecular and Microbial Biosciences, The University of Sydney (Australia)
- Programs in Gene Function and Expression and Molecular Medicine, University of Massachusetts Medical School (United States)
An intramolecular complex comprising the LIM domains of Lhx3 and the interacting domain of Isl1 tethered by a flexible linker was engineered, overexpressed in E. coli, purified and crystallized. A stable intramolecular complex comprising the LIM domains of the LIM-homeodomain protein Lhx3 tethered to a peptide region of Isl1 has been engineered, purified and crystallized. The monoclinic crystals belong to space group C2, with unit-cell parameters a = 119, b = 62.2, c = 51.9 Å, β = 91.6°, and diffract to 2.05 Å resolution.
- OSTI ID:
- 22360507
- Journal Information:
- Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: Pt 4 Vol. 64; ISSN ACSFCL; ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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