Structural heterogeneity in protein crystals.

  title={Structural heterogeneity in protein crystals.},
  author={Janet L. Smith and Wayne A. Hendrickson and Richard B Honzatko and Scott Sheriff},
  volume={25 18},
Extensive conformational heterogeneity is reported in highly refined crystallographic models for the proteins crambin, erabutoxin, myohemerythrin, and lamprey hemoglobin. From 6% to 13% of the amino acid side chains of these four proteins are seen in multiple, discrete conformations. Most common are flexible side chains on the molecular surface, but structural heterogeneity occasionally extends to buried side chains or to the polypeptide backbone. A few instances of sequence heterogeneity are… CONTINUE READING

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