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Crystallization and preliminary X-ray crystallographic analysis of the 30 kDa membrane-binding domain of protein 4.1 from human erythrocytes.
Han, B G; Nunomura, W; Wu, H; Mohandas, N; Jap, B K.
Afiliação
  • Han BG; Life Sciences Division, Lawrence Berkeley National Laboratory, University of California, Berkeley, California 94720, USA.
Acta Crystallogr D Biol Crystallogr ; 56(Pt 2): 187-8, 2000 Feb.
Article em En | MEDLINE | ID: mdl-10666600
ABSTRACT
The 30 kDa membrane-binding domain of protein 4.1 from human erythrocytes has been expressed in Escherichia coli and crystallized in a form suitable for X-ray crystallographic study. Crystals were grown using a salting-in technique. Crystals have a tetragonal plate shape and belong to the C2 space group, with unit-cell parameters a = 163.9, b = 106.5, c = 93.5 A, beta = 95.5 degrees. The crystals diffract to 2.8 A resolution.
Assuntos
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Base de dados: MEDLINE Assunto principal: Neuropeptídeos / Proteínas do Citoesqueleto / Membrana Eritrocítica / Proteínas de Membrana Idioma: En Ano de publicação: 2000 Tipo de documento: Article
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Base de dados: MEDLINE Assunto principal: Neuropeptídeos / Proteínas do Citoesqueleto / Membrana Eritrocítica / Proteínas de Membrana Idioma: En Ano de publicação: 2000 Tipo de documento: Article