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 ligand 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 P21212 with unit-cell dimensions of a = 207.4, b = 113.3 and c = 120.4 A. A native data set has been recorded and a heavy-atom search is currently under way. Diffraction from these crystals, however, is limited to low resolution and extensive trials to improve crystal quality further have all failed. To analyse the molecular shape and aggregation of the receptor protein in solution, small-angle 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.
Universitäts-Krankenhaus Eppendorf, Institut f. Phys. Chemie, c/o DESY, Geb. 22a, Notkestrasse 85, 22603 Hamburg, Germany.
M
M
Degenhardt
W
W
Weber
S
S
Eschenburg
K
K
Dierks
S S
SS
Funari
G
G
Rapp
C
C
Betzel
D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods; D066246:ErbB Receptors / Q000737:chemistry* / Q000302:isolation & purification; D008027:Light; D051379:Mice; D010446:Peptide Fragments / Q000737:chemistry* / Q000302:isolation & purification; D011487:Protein Conformation; D012542:Scattering, Radiation
D010446:Peptide Fragments; D066246:ErbB Receptors