Crystallographic characterization of a stress-induced multifunctional protein, rat HBP-23. |
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| Authors: | S Hirotsu Y Abe N Nagahara H Hori T Nishino K Okada T Hakoshima |
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| Affiliation: | Department of Molecular Biology, Nara Institute of Science and Technology (NAIST), 8916-5 Takayama, Nara, Ikoma, 630-01, Japan. |
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| Abstract: | HBP-23 is a stress-induced multifunctional rat protein that belongs to a novel family of antioxidant proteins, referred to as peroxiredoxins, and exhibits heme-binding and inhibition of c-Abl protein tyrosine kinase. Recombinant HBP-23 was crystallized by a hanging-drop vapor-diffusion method. The crystals belong to space group P41212 or P43212 with unit-cell dimensions of a = b = 73.47 A, c = 210.37 A and contain two protein molecules in the asymmetric unit. A data set at 2.7-A resolution was collected with a cryo-crystallographic technique. Crystals of selenomethionyl HBP-23 were also obtained under the same conditions. |
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