
Crystallization of an Lhx3–Isl1 complex
Author(s) -
Bhati Mugdha,
Lee Mihwa,
Nancarrow Amy Louise,
Bach Ingolf,
Guss J. Mitchell,
Matthews Jacqueline Mary
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430910800691x
Subject(s) - crystallization , monoclinic crystal system , crystallography , lim domain , resolution (logic) , chemistry , materials science , topology (electrical circuits) , gene , crystal structure , combinatorics , biochemistry , mathematics , computer science , transcription factor , organic chemistry , artificial intelligence , zinc finger
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 C 2, with unit‐cell parameters a = 119, b = 62.2, c = 51.9 Å, β = 91.6°, and diffract to 2.05 Å resolution.