Expression purification crystallization and preliminary X-ray crystallographic analysis of the SH3 domain of human AHI1

摘要

The SH3 domain of human AHI1 was cloned and expressed in Escherichia coli. The protein was purified by affinity and size-exclusion chromatography and was crystallized using the sitting-drop vapour-diffusion method at 293 K. A complete data set was collected to 2.5 Å resolution at 110 K. The crystal belonged to space group P41212, with unit-cell parameters a = 67.377, b = 67.377, c = 98.549 Å.