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Optimization of Crystals of an Inhibitory Antibody of Urokinase Plasminogen Activator Receptor (uPAR) with Hydrogen Peroxide and Low Protein Concentration

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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 P212121 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.
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Keywords: antibody; crystal optimization; hydrogen peroxide; upar

Document Type: Review Article

Affiliations: State Key Laboratory of Structural Chemistry, Fujian Institute of Research on the Structure of Matter, The Graduate School of Chinese Academy of Sciences, Chinese Academy of Sciences, Fuzhou 350002, People's Republic of China;

Publication date: 2005-10-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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