Crystallization and preliminary crystallographic analysis of two endo-beta-N-acetylglucosaminidases, endo H and endo F1.
Crystallization and preliminary crystallographic analysis of two endo-beta-N-acetylglucosaminidases, endo H and endo F1.
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两种内切-β-N-乙酰氨基葡萄糖苷酶（endo H 和 end F1）的结晶和初步晶体学分析。
DOI：
10.1006/jmbi.1994.1214
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发表时间：
1994
影响因子：
5.6
通讯作者：
Guan,C
中科院分区：
文献类型：
--
作者：
VanRoey,P;Silva,GH;Rao,V;PlummerJr,TH;Tarentino,AL;Guan,C
Endo H和F1是内切糖苷酶，通过水解N，N′-二乙酰壳二糖核心的糖苷键切割天冬酰胺连接的糖蛋白的寡糖部分。这两种酶对高甘露糖寡糖具有特异性。在这里，我们报告了Endo H和Endo F1的结晶和初步晶体学分析。采用悬滴气相扩散法生长晶体。两种蛋白质均从含有聚乙二醇8000和乙酸锌作为二甲胂酸盐缓冲液中的沉淀剂的结晶缓冲液中结晶。Endo H晶体属于四面体空间群P41212（或P43212），晶胞尺寸为：a= 85·22 nm，c= 89·41 nm。Endo F1晶体属六方晶系，空间群为P61（或P65），晶胞尺寸为：a= 70·61 nm，c= 100·32 nm。这两种蛋白质的晶体均具有至少1·8 μ m的分辨率。
Endo H and F1are endoglycosidases that cleave the oligosaccharide moiety of asparagine-linked glycoproteins by hydrolysis of the glycosidic bond in theN,N′-diacetylchitobiose core. The two enzymes are specific for high-mannose oligosaccharides. Here, we report the crystallization and preliminary crystallographic analysis of Endo H and Endo F1. Crystals were grown by hanging drop vapor diffusion methods. Both proteins crystallize from crystallization buffers containing polyethyleneglycol 8000 and zinc acetate as precipitating agents in cacodylate buffer. The crystals of Endo H belong to the tetragonal space group P41212 (orP43212) with cell dimensions:a= 85·22 Å,c= 89·41 Å. The crystals of Endo F1belong to the hexagonal space groupP61(orP65) with cell dimensions:a= 70·61 Å,c= 100·32 Å. Crystals of both proteins diffract to at least 1·8 Å resolution.