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Protein crystallization benefits from the rough well surface of a 48-well polystyrene microplate

Ye, Zhao-yang ; Broströmer, Erik LU ; Nan, Jie LU ; Cao, Xiao-fang ; Liu, Xiang ; Qiao, Li ; Liu, Zhong-jing and Su, Xiao-dong LU (2019) In Journal of Crystal Growth 532. p.125425-125425
Abstract
It’s not clear whether the drop well surface can induce heterogeneous nucleation to increase the probability of screening success, although a medium-throughput 48-well SBS (the Society for Biomolecular Screening, USA) polystyrene microplate has been widely used for protein crystallization screening. Here, our accumulating data suggested that this 48-well SBS microplate with rough surface is beneficial for protein crystallization. It was observed that some protein crystals were only formed on the rough edges and/or walls of the drop well, but not on the flat bottom or in the crystallization drop. It was further demonstrated with two standard test proteins. The protuberances, grooves and cavities with varied sizes and shapes at... (More)
It’s not clear whether the drop well surface can induce heterogeneous nucleation to increase the probability of screening success, although a medium-throughput 48-well SBS (the Society for Biomolecular Screening, USA) polystyrene microplate has been widely used for protein crystallization screening. Here, our accumulating data suggested that this 48-well SBS microplate with rough surface is beneficial for protein crystallization. It was observed that some protein crystals were only formed on the rough edges and/or walls of the drop well, but not on the flat bottom or in the crystallization drop. It was further demonstrated with two standard test proteins. The protuberances, grooves and cavities with varied sizes and shapes at micrometer-scale in the rough drop well wall can serve as nucleants and induce heterogeneous nucleation of protein crystals. The rough wall microplate provides a potent tool for protein crystallographers embarking on crystallization trials. (Less)
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author
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publishing date
type
Contribution to journal
publication status
published
in
Journal of Crystal Growth
volume
532
pages
125425 - 125425
publisher
Elsevier
external identifiers
  • scopus:85076685506
ISSN
0022-0248
DOI
10.1016/j.jcrysgro.2019.125425
language
English
LU publication?
no
id
0fc8d6e2-4944-46ef-821e-6f1e1a482961
alternative location
https://linkinghub.elsevier.com/retrieve/pii/S0022024819306402
date added to LUP
2020-02-13 16:42:37
date last changed
2022-04-18 20:36:49
@article{0fc8d6e2-4944-46ef-821e-6f1e1a482961,
  abstract     = {{It’s not clear whether the drop well surface can induce heterogeneous nucleation to increase the probability of screening success, although a medium-throughput 48-well SBS (the Society for Biomolecular Screening, USA) polystyrene microplate has been widely used for protein crystallization screening. Here, our accumulating data suggested that this 48-well SBS microplate with rough surface is beneficial for protein crystallization. It was observed that some protein crystals were only formed on the rough edges and/or walls of the drop well, but not on the flat bottom or in the crystallization drop. It was further demonstrated with two standard test proteins. The protuberances, grooves and cavities with varied sizes and shapes at micrometer-scale in the rough drop well wall can serve as nucleants and induce heterogeneous nucleation of protein crystals. The rough wall microplate provides a potent tool for protein crystallographers embarking on crystallization trials.}},
  author       = {{Ye, Zhao-yang and Broströmer, Erik and Nan, Jie and Cao, Xiao-fang and Liu, Xiang and Qiao, Li and Liu, Zhong-jing and Su, Xiao-dong}},
  issn         = {{0022-0248}},
  language     = {{eng}},
  month        = {{12}},
  pages        = {{125425--125425}},
  publisher    = {{Elsevier}},
  series       = {{Journal of Crystal Growth}},
  title        = {{Protein crystallization benefits from the rough well surface of a 48-well polystyrene microplate}},
  url          = {{http://dx.doi.org/10.1016/j.jcrysgro.2019.125425}},
  doi          = {{10.1016/j.jcrysgro.2019.125425}},
  volume       = {{532}},
  year         = {{2019}},
}