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Bovine P2 Myelin Basic Protein Crystallizes in Three Different Forms
Author(s) -
Sedzik Jan,
Bergfors Terese,
Jones T. Alwyn,
Weise Michael
Publication year - 1988
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1988.tb02496.x
Subject(s) - ammonium sulfate , resolution (logic) , peg ratio , myelin , crystallography , chemistry , molecule , myelin basic protein , biology , chromatography , central nervous system , organic chemistry , computer science , finance , artificial intelligence , neuroscience , economics
P2 protein is a minor component of the myelin membrane. We have crystallized this protein for high‐resolution crystallographic study. Three crystal morphologies are available. Two of them are from ammonium sulfate, and one is from polyethyleneglycol (PEG). The unit cell of the most suitable crystals from PEG 4000 has the dimensions a = 91.3 Å, b = 99.8 Å, c = 56.0 Å; is of space group P2 1 2 1 2 1 ; and contains up to four molecules per asymmetric unit. The limit of resolution is 2.7 Å.