Article info Vol. 6  No. 1   pp.  28 ~ 31
Title Crystallization and preliminary diffraction analysis of dual specificity phosphatase 13a
Authors Hee Gyeong Min, Tae Jin Jeon, Chun Hwa Wei, Myungbin Kim and Seong Eon Ryu*
Institutions Department of Bioengineering, College of Engineering, Hanyang University, Seoul, Korea *Correspondence: ryuse@hanyang.ac.kr
Abstract Dual specificity phosphatases (DUSPs) include MAP kinase phosphatases and atypical dual specificity phosphatases, and mediate cell growth and differentiation. They are considered as drug targets against cancers, diabetes, immune diseases, and neuronal diseases. Two different DUSPs, DUSP13a and DUSP13b are coded in one gene (DUSP13) whose alternative splicing results in two sequence-related proteins with different target specificities. The crystal structure of DUSP13b showed a canonical DUSP fold. However, the structure of DUSP13a has not been determined yet. To understand structural mechanism of distinctive target specificities of sequence-related DUSPs, we prepared diffraction-quality crystals of DUSP13a. Cysteine residues in DUSP13a gene were mutated to serine or alanine to prevent cysteine oxidation. From the stabilized protein, we were able to grow good crystals that diffracted to 1.7 Å resolution. The preliminary diffraction analysis revealed that the crystal is in the space group P21 with unit cell parameters of a = 40.04 Å, b = 89.34 Å, c = 45.90 Å, α = 90.00°, β = 89.87° and γ = 90.00°.