Crystallization and diffraction of an Lhx4-Isl2 complex.
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 P2(1), with unit-cell parameters a = 46.8, b = 88.7, c = 49.9 A, beta = 111.9 degrees, and diffracted to 2.16 A resolution.
Gadd
Morgan S
MS
School of Molecular and Microbial Biosciences, University of Sydney, Australia.
Langley
David B
DB
Guss
J Mitchell
JM
Matthews
Jacqueline M
JM
D000818:Animals; D003460:Crystallization; D018398:Homeodomain Proteins / Q000737:chemistry* / Q000378:metabolism*; D060850:LIM-Homeodomain Proteins; D051379:Mice; D009046:Motor Neurons / Q000737:chemistry / Q000378:metabolism; D009419:Nerve Tissue Proteins / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding / Q000502:physiology; D015202:Protein Engineering / Q000379:methods; D014157:Transcription Factors / Q000737:chemistry* / Q000378:metabolism*; D014961:X-Ray Diffraction
D018398:Homeodomain Proteins; C558561:Isl2 protein, mouse; D060850:LIM-Homeodomain Proteins; C108538:Lhx4 protein, mouse; D009419:Nerve Tissue Proteins; D014157:Transcription Factors; C063843:insulin gene enhancer binding protein Isl-1