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

人AHI1的SH3结构域的表达、纯化、结晶和初步X射线晶体学分析

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Abstract

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 A resolution at 110 K. The crystal belonged to space group P4(1)2(1)2, with unit-cell parameters a = 67.377, b = 67.377, c = 98.549 A.

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