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PDBsum entry 2zrs
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References listed in PDB file
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Key reference
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Title
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Crystallization and X-Ray diffraction analysis of n-Terminally truncated human alg-2.
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Authors
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H.Suzuki,
M.Kawasaki,
T.Kakiuchi,
H.Shibata,
S.Wakatsuki,
M.Maki.
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Ref.
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Acta Crystallogr Sect F Struct Biol Cryst Commun, 2008,
64,
974-977.
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PubMed id
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Abstract
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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 mM MES pH 6.5, 12.5%(v/v) 2-propanol and 150 mM calcium
acetate or 100 mM MES pH 6.0, 15%(v/v) ethanol and 200 mM zinc acetate. Crystals
of the Ca(2+)-bound form belonged to space group P2(1)2(1)2(1), with unit-cell
parameters a = 54.8, b = 154.4, c = 237.7 A, alpha = beta = gamma = 90 degrees ,
and diffracted to 3.1 A resolution. Crystals of the Zn(2+)-bound form belonged
to space group P2(1)2(1)2(1), with unit-cell parameters a = 52.8, b = 147.5, c =
230.7 A, alpha = beta = gamma = 90 degrees , and diffracted to 3.3 A 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.
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