Open AccessCrystallization and X‐ray diffraction analysis of N‐terminally truncated human ALG‐2
Author(s) -
Suzuki Hironori,
Kawasaki Masato,
Kakiuchi Takeshi,
Shibata Hideki,
Wakatsuki Soichi,
Maki Masatoshi
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108030297
Subject(s) - crystallography , crystallization , diffraction , molecule , resolution (logic) , x ray crystallography , chemistry , metal , molecular replacement , crystal structure , stereochemistry , physics , optics , organic chemistry , artificial intelligence , computer science
ALG‐2 (apoptosis‐linked gene 2) is an apoptosis‐linked calcium‐binding protein with five EF‐hand motifs in the C‐terminal region. N‐terminally truncated ALG‐2 (des3‐23ALG‐2) was crystallized by the vapour‐diffusion method in buffer consisting of either 50 m M MES pH 6.5, 12.5%( v / v ) 2‐propanol and 150 m M calcium acetate or 100 m M MES pH 6.0, 15%( v / v ) ethanol and 200 m M zinc acetate. Crystals of the Ca 2+ ‐bound form belonged to space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 54.8, b = 154.4, c = 237.7 Å, α = β = γ = 90°, and diffracted to 3.1 Å resolution. Crystals of the Zn 2+ ‐bound form belonged to space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 52.8, b = 147.5, c = 230.7 Å, α = β = γ = 90°, and diffracted to 3.3 Å resolution. The structures of the Ca 2+ ‐bound form and the Zn 2+ ‐bound form were solved by the molecular‐replacement method. Although both crystals contained eight ALG‐2 molecules per asymmetric unit, the metal‐ion locations and octameric arrangements were found to be significantly different.