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Derewenda, Z.S. and Godzik, A. (2017) The “Sticky Patch” Model of Crystallization and Modification of Proteins for Enhanced Crystallizability. In: Wlodawer, A., Dauter, Z. and Jaskolski, M., Eds., Protein Crystallography. Methods in Molecular Biology, Humana Press, New York, 77-115.
https://doi.org/10.1007/978-1-4939-7000-1_4

has been cited by the following article:

• TITLE: Correlating Combined Features of Amino Acid and Protein with Crystallization Propensity of Proteins from Mycobacterium tuberculosis

  AUTHORS: Shaomin Yan, Guang Wu

  KEYWORDS: Protein Feature, Mycobacterium tuberculosis, Protein Crystallization

  JOURNAL NAME: Journal of Biomedical Science and Engineering, Vol.12 No.9, September 29, 2019

  ABSTRACT: Since a decade ago, both protein and amino acid features have been correlated with crystallization propensity of proteins in order to develop methods to predict whether a protein can be crystallized. In this continuing study, each of three features combining features of amino acid and protein, was correlated with the crystallization propensity of proteins from Mycobacterium tuberculosis using logistic and neural network models. The results showed that two combined features, amino acid distribution probability and future composition, had good predictions on whether a protein would be crystallized in comparison with the predictions obtained from each of 531 amino acid features. The results obtained from the third combined feature, amino acid pair predictability, demonstrated the trend of crystallization propensity in proteins from Mycobacterium tuberculosis.