CRYSTALLIZATION AND PRELIMINARY-X-RAY CRYSTALLOGRAPHIC ANALYSIS OF THE EGF RECEPTOR ECTODOMAIN

Crystallization of the hydrophilic ectodomain of the epidermal growth factor (EGF) receptor has been accomplished in the presence of the lig and EGF. Two different crystal forms have been obtained, one of which was suitable for X-ray analysis. The space group of this form has been assigned to P2(1)2(1)2 with unit-cell dimensions of a = 207.4, b = 11 3.3 and c = 120.4 Angstrom. A native data set has been recorded and a heavy-atom search is currently under way. Diffraction from these cryst als, however, is limited to low resolution and extensive trials to imp rove crystal quality further have all failed. To analyse the molecular shape and aggregation of the receptor protein in solution, small-angl e X-ray diffraction and dynamic light-scattering techniques have been applied. Synchrotron radiation in combination with cryo-techniques is essential for data collection because of the high solvent content and radiation sensitivity.