Crystallographic characterization of a stress-induced multifunctional protein, rat HBP-23

Citation
S. Hirotsu et al., Crystallographic characterization of a stress-induced multifunctional protein, rat HBP-23, J STRUCT B, 126(1), 1999, pp. 80-83
Citations number
24
Categorie Soggetti
Biochemistry & Biophysics
Journal title
JOURNAL OF STRUCTURAL BIOLOGY
ISSN journal
10478477 → ACNP
Volume
126
Issue
1
Year of publication
1999
Pages
80 - 83
Database
ISI
SICI code
1047-8477(19990601)126:1<80:CCOASM>2.0.ZU;2-I
Abstract
HBP-23 is a stress-induced multifunctional rat protein that belongs to a no vel family of antioxidant proteins, referred to as peroxiredoxins, and exhi bits heme-binding and inhibition of c-Abl protein tyrosine kinase. Recombin ant HBP-23 was crystallized by a hanging-drop vapor-diffusion method. The c rystals belong to space group P4(1)2(1)2 or P4(3)2(1)2 with unit-cell dimen sions of a = b = 73.47 Angstrom, c = 210.37 Angstrom and contain two protei n molecules in the asymmetric unit. A data set at 2.7-Angstrom resolution w as collected with a cryo-crystallographic technique. Crystals of selenometh ionyl HBP-23 were also obtained under the same conditions. (C) 1999 Academi c Press.