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Crystallization and preliminary cryogenic X‐ray diffraction analyses of protein L‐isoaspartyl O ‐methyltransferase from human fetal brain
Author(s) -
Smith Craig D.,
Barchue Joseph,
Mentel Charles,
Delucas Lawrence,
Shirasawa Takuji,
Chattopadhyay Debasish
Publication year - 1997
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/(sici)1097-0134(199707)28:3<457::aid-prot15>3.0.co;2-g
Subject(s) - recombinant dna , methyltransferase , fetus , crystallization , human brain , diffraction , crystallography , chemistry , microbiology and biotechnology , methylation , materials science , biology , biochemistry , optics , pregnancy , physics , gene , neuroscience , genetics , organic chemistry
Recombinant human fetal brain protein L‐isoaspartyl O‐methyltransferase, EC 2.1.1.77, was crystallized in PEG 8000 with adenosine homocysteine by a macroseeding technique. The space group was P2 1 with a = 47.4 Å, b = 53.9 Å, c = 48.7 Å and β = 116.4° for cryofrozen crystals at 90 K. The crystals diffracted to 2.1 Å and have one molecule per asymmetric unit. Proteins 28:457–460, 1997. © 1997 Wiley‐Liss, Inc.