Open AccessCrystallization and preliminary crystallographic study of carnosinase CN2 from mice
Author(s) -
Yamashita Tetsuo,
Unno Hideaki,
Ujita Sayuri,
Otani Hiroto,
Nagai Katsuya,
Okumura Nobuaki,
HashidaOkumura Akiko,
Kusunoki Masami
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106034701
Subject(s) - monoclinic crystal system , crystallography , crystallization , x ray crystallography , crystal structure , diffraction , space group , materials science , chemistry , optics , physics , organic chemistry
Mammalian tissues contain several histidine‐containing dipeptides, of which l ‐carnosine is the best characterized and is found in various tissues including the brain and skeletal muscles. However, the mechanism for its biosynthesis and degradation have not yet been fully elucidated. Crystallographic study of carnosinase CN2 from mouse has been undertaken in order to understand its enzymatic mechanism from a structural viewpoint. CN2 was crystallized by the hanging‐drop vapour‐diffusion technique using PEG 3350 as a precipitant. Crystals were obtained in complex with either Mn 2+ or Zn 2+ . Both crystals of CN2 belong to the monoclinic space group P 2 1 and have almost identical unit‐cell parameters ( a = 54.41, b = 199.77, c = 55.49 Å, β = 118.52° for the Zn 2+ complex crystals). Diffraction data were collected to 1.7 and 2.3 Å for Zn 2+ and Mn 2+ complex crystals, respectively, using synchrotron radiation. Structure determination is ongoing using the multiple‐wavelength anomalous diffraction (MAD) method.