Expression, purification, crystallization and crystallographic characterization of the human MHC class I related protein MICA
Expression, purification, crystallization and crystallographic characterization of the human MHC class I related protein MICA
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DOI：
10.1107/s0907444997015229
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发表时间：
1998-05-01
期刊：
影响因子：
--
通讯作者：
Strong, RK
中科院分区：
文献类型：
--
作者：
Bauer, S;Willie, ST;Strong, RK
人类 MHC 编码分子 MICA（MHC I 类蛋白的同源物）的晶体已在悬滴蒸气扩散试验中生长，使用硫酸铵作为沉淀剂，并在基于杆状病毒的系统中表达重组蛋白。冷冻保存的 MICA 晶体属于立方空间群 F4(1)32，晶格常数 a = b = c = 260.7 埃，冷冻保存时衍射分辨率极限为 3.0 埃。当以常规方式处理时，这些晶体不会发生衍射。
Crystals of the human MHC-encoded molecule MICA, a homologue of MHC class I proteins, have been grown in hanging-drop vapor-diffusion trials using ammonium sulfate as a precipitating agent with recombinant protein expressed in a baculovirus-based system. Cryo-preserved crystals of MICA belong to the cubic space group F4(1)32 with lattice constants a = b = c = 260.7 Angstrom and diffract to a resolution limit of 3.0 Angstrom when cryo-preserved. These crystals do not diffract when handled conventionally.