Literature DB >> 2453613

Bovine P2 myelin basic protein crystallizes in three different forms.

J Sedzik1, T Bergfors, T A Jones, M Weise.   

Abstract

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 A, b = 99.8 A, c = 56.0 A; 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 A.

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Year:  1988        PMID: 2453613     DOI: 10.1111/j.1471-4159.1988.tb02496.x

Source DB:  PubMed          Journal:  J Neurochem        ISSN: 0022-3042            Impact factor:   5.372


  3 in total

1.  Purification of P0 myelin glycoprotein by a Cu2+-immobilized metal affinity chromatography.

Authors:  J Sedzik; Y Kotake; K Uyemura
Journal:  Neurochem Res       Date:  1999-06       Impact factor: 3.996

2.  Expression and cross-species reactivity of fatty acid-binding protein of Clonorchis sinensis.

Authors:  Ji-Sook Lee; Tai-Soon Yong
Journal:  Parasitol Res       Date:  2004-06-09       Impact factor: 2.289

3.  Is myelin basic protein crystallizable?

Authors:  J Sedzik; D A Kirschner
Journal:  Neurochem Res       Date:  1992-02       Impact factor: 3.996

  3 in total

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