{'fraction_non_alphanumeric': 0.023732470334412083, 'fraction_numerical': 0.010787486515641856, 'mean_word_length': 4.658536585365853, '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}}
X‐ray Crystal Structures of the E. coli 70S ribosome at 3.5 Å resolution

We are using x‐ray crystallography to probe the structural basis for the many aspects of protein biosynthesis that require the intact ribosome. Our goal is to make an atomic‐resolution “movie” of a ribosome in the process of making a protein. We have obtained crystals of the entire E. coli ribosome that diffract x‐rays to a resolution of 3.1–3.2 Å. We are now refining ribosome structural models at a resolution of 3.5 Å. These models reveal possible mechanisms for mRNA and tRNA translocation, the nature of the ribosomal subunit interface, and structural features in the peptidyl transferase center that may be important for catalysis. Moreover, we are using these crystals to probe in atomic detail the effects of antibiotics on the full ribosome and mutations in the ribosome that lead to antibiotic resistance or perturb key steps in translation.