Optimization of crystals of an inhibitory antibody of urokinase plasminogen activator receptor (uPAR) with hydrogen peroxide and low protein concentration

Yongdong Li, Xiaoli Shi, Graham Parry, Liqing Chen, Jennifer A. Callahan, Andrew P. Mazar, Mingdong Huang*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

1 Scopus citations

Abstract

Optimization of protein crystal formation is often a necessary step leading to diffraction-quality crystals to enable collection of a full X-ray data set. Typical protein crystal optimization involves screening different components, e.g., pH, precipitants, and additives of the precipitant solution. Here we present an example using an inhibitory antibody of urokinase plasminogen activator receptor (uPAR) where such procedures did not yield diffracting crystals. In contrast, it was the treatment of the protein with hydrogen peroxide incubation and the protein concentration reduction that were found to be key factors in obtaining diffracting crystals. Final crystals diffracted to 1.75 Å, and belong to orthorhombic P21212 1 space group with unit cell parameters a=37.162 Å, b=84.474 Å, c=134.030 Å, and contain one molecule of Fab fragment of anti-uro kinase receptor antibody in the asymmetric unit.

Original languageEnglish (US)
Pages (from-to)655-658
Number of pages4
JournalProtein and Peptide Letters
Volume12
Issue number7
DOIs
StatePublished - Oct 1 2005

Keywords

  • Antibody
  • Crystal optimization
  • Hydrogen peroxide
  • uPAR

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry

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