Protein Science, Vol 6, Issue 12 2663-2666, Copyright © 1997 by Cold Spring Harbor Laboratory Press

FOR THE RECORD

Crystallization of the first three domains of the human insulin-like growth factor-1 receptor

N. M. MCKERN, M. LOU, M. J. FRENKEL, A. VERKUYLEN, J. D. BENTLEY, G. O. LOVRECZ, N. IVANCIC, T. C. ELLEMAN, TPJ. GARRETT, L. J. COSGROVE and C. W. WARD
CSIRO Division of Molecular Science, 343 Royal Parade, Parkville, Victoria, 3052 Australia

The insulin-like growth factor-1 receptor (IGF-1R) is a tyrosine kinase receptor of central importance in cell proliferation. A fragment (residues 1-462) comprising the L1-cysteine rich-L2 domains of the human IGF-1R ectodomain has been overexpressed in glycosylation-deficient Lec8 cells and has been affinity-purified via a c-myc tag followed by gel filtration. The fragment was recognized by two anti-IGF-1R monoclonal antibodies, 24-31 and 24-60, but showed no detectable binding of IGF-1 or IGF-2. Isocratic elution of IGF-1R/462 on anion-exchange chromatography reduced sample heterogeneity, permitting the production of crystals that diffracted to 2.6 A resolution with cell dimensions a = 77.0 A, b = 99.5 A, c = 120.1 A, and space group P2(1)2(1)2(1).
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