1rb7 Citations

Microseed matrix screening to improve crystals of yeast cytosine deaminase.

Acta Crystallogr D Biol Crystallogr 60 601-5 (2004)
Cited: 22 times
EuropePMC logo PMID: 14993707

Abstract

A crystallization strategy termed 'microseed matrix screening' is described where the optimal conditions for nucleation versus extended lattice growth are not compatible. This method is an extension of conventional seeding techniques in which microseeds from the nucleation step are systematically seeded into new conditions where all components of the drop are allowed to vary to screen for subsequent growth of well ordered specimens. The structure of a crystal form of yeast cytosine deaminase produced by streak-seeding using a single condition for both nucleation and growth is compared with the structure of a related crystal form produced by separating nucleation and growth conditions. The resulting structural comparison demonstrates that differential chelation patterns of cations by acidic surface residues of proteins within crystal lattice contacts is a critical parameter of crystal nucleation and growth.

Reviews citing this publication (3)

  1. Automated technologies and novel techniques to accelerate protein crystallography for structural genomics. Manjasetty BA, Turnbull AP, Panjikar S, Büssow K, Chance MR. Proteomics 8 612-625 (2008)
  2. A historical perspective on protein crystallization from 1840 to the present day. Giegé R. FEBS J 280 6456-6497 (2013)
  3. Emerging implications of nonmammalian cytosine deaminases on cancer therapeutics. Yata VK, Gopinath P, Ghosh SS. Appl Biochem Biotechnol 167 2103-2116 (2012)

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  17. Capillary-seeding crystallization and preliminary crystallographic analysis of a solvent-tolerant elastase from Pseudomonas aeruginosa strain K. Ali MS, Said ZS, Rahman RN, Chor AL, Basri M, Salleh AB. Int J Mol Sci 14 17608-17617 (2013)
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  19. Induced conformational change in human IL-4 upon binding of a signal-neutralizing DARPin. Obmolova G, Teplyakov A, Malia TJ, Keough E, Luo J, Sweet R, Jacobs SA, Yi F, Hippensteel R, O'Neil KT, Gilliland GL. Proteins 83 1191-1197 (2015)