{'fraction_non_alphanumeric': 0.0497131931166348, 'fraction_numerical': 0.06118546845124283, 'mean_word_length': 4.458333333333333, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
Expression, purification, crystallization and preliminary X-ray crystallographic analysis of the SH3 domain of human AHI1.

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.