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与抗体Fab片段复合的B型流感病毒神经氨酸酶的结晶及初步X射线分析。

Crystallization and preliminary X-ray analysis of type B influenza virus neuraminidase complexed with antibody Fab fragments.

作者信息

Laver W G, Luo M, Bossart P J, Babu Y S, Smith C, Accavitti M A, Tulloch P A, Air G M

机构信息

John Curtin School of Medical Research, Australian National University, Canberra City.

出版信息

Virology. 1988 Dec;167(2):621-4.

PMID:3201756
Abstract

Fab fragments from four different monoclonal antibodies have been complexed with influenza B virus neuraminidase (B/Lee/40) and the complexes have been crystallized. Three of the complex crystals are, so far, not suitable for X-ray diffraction studies, but the fourth (B/Lee/40 NA-B1Fab) forms large crystals which diffract X-rays to 3.0 A resolution. The crystals have a space group of F432, a = 441.21 A. Vm calculations show that the asymmetric unit contains two monomeric complexes.

摘要

来自四种不同单克隆抗体的Fab片段已与乙型流感病毒神经氨酸酶(B/Lee/40)复合,并且这些复合物已结晶。到目前为止,其中三种复合晶体不适合进行X射线衍射研究,但第四种(B/Lee/40 NA-B1Fab)形成了大晶体,其X射线衍射分辨率达到3.0埃。这些晶体的空间群为F432,a = 441.21埃。Vm计算表明,不对称单元包含两个单体复合物。

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