Literature DB >> 18218713

Rationalizing alpha-helical membrane protein crystallization.

Simon Newstead1, Sébastien Ferrandon, So Iwata.   

Abstract

X-ray crystallography is currently the most successful method for determining the three-dimensional structure of membrane proteins. Nevertheless, growing the crystals required for this technique presents one of the major bottlenecks in this area of structural biology. This is especially true for the alpha-helical type membrane proteins that are of particular interest due to their medical relevance. To address this problem we have undertaken a detailed analysis of the crystallization conditions from 121 alpha-helical membrane protein structures deposited in the Protein Data Bank. This information has been analyzed so that the success of different parameters can be easily compared for different membrane protein families. Concurrent with this analysis, we also present the new sparse matrix crystallization screen MemGold.

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Year:  2008        PMID： 18218713      PMCID： PMC2248303          DOI： 10.1110/ps.073263108

Source DB:  PubMed          Journal:  Protein Sci        ISSN： 0961-8368            Impact factor:   6.725


  16 in total

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10.  Influence of divalent cations in protein crystallization.

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  68 in total

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Journal:  Langmuir       Date:  2010-06-01       Impact factor: 3.882

Review 2.  New amphiphiles for membrane protein structural biology.

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Journal:  Acta Biomater       Date:  2020-06-06       Impact factor: 8.947

4.  Phasing statistics for alpha helical membrane protein structures.

Authors:  Joanne L Parker; Simon Newstead
Journal:  Protein Sci       Date:  2013-09-17       Impact factor: 6.725

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6.  Maltose neopentyl glycol-3 (MNG-3) analogues for membrane protein study.

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7.  Current trends in α-helical membrane protein crystallization: an update.

Authors:  Joanne L Parker; Simon Newstead
Journal:  Protein Sci       Date:  2012-08-10       Impact factor: 6.725

Review 8.  Crystallizing membrane proteins using lipidic bicelles.

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9.  An Improved Strategy for Fluorescent Tagging of Membrane Proteins for Overexpression and Purification in Mammalian Cells.

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10.  Characterization of protein detergent complexes by NMR, light scattering, and analytical ultracentrifugation.

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