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Protein Crystallizability.

Authors
  • Smialowski, Pawel1
  • Wong, Philip2
  • 1 Biomedical Center Munich, Ludwig-Maximilians-University, Großhaderner Strasse 9, 82152, Martinsried, Germany. [email protected] , (Germany)
  • 2 Biomedical Center Munich, Ludwig-Maximilians-University, Großhaderner Strasse 9, 82152, Martinsried, Germany. , (Germany)
Type
Published Article
Journal
Methods in molecular biology (Clifton, N.J.)
Publication Date
Jan 01, 2016
Volume
1415
Pages
341–370
Identifiers
DOI: 10.1007/978-1-4939-3572-7_17
PMID: 27115641
Source
Medline
Keywords
Language
English
License
Unknown

Abstract

Obtaining diffracting quality crystals remains a major challenge in protein structure research. We summarize and compare methods for selecting the best protein targets for crystallization, construct optimization and crystallization condition design. Target selection methods are divided into algorithms predicting the chance of successful progression through all stages of structural determination (from cloning to solving the structure) and those focusing only on the crystallization step. We tried to highlight pros and cons of different approaches examining the following aspects: data size, redundancy and representativeness, overfitting during model construction, and results evaluation. In summary, although in recent years progress was made and several sequence properties were reported to be relevant for crystallization, the successful prediction of protein crystallization behavior and selection of corresponding crystallization conditions continue to challenge structural researchers.

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