A new crystal form of tropomyosin. Preliminary X-ray diffraction analysis.
A new crystal form of tropomyosin. Preliminary X-ray diffraction analysis.
复制标题
原肌球蛋白的新晶型。
DOI：
10.1016/0022-2836(87)90339-1
复制
发表时间：
1987
影响因子：
5.6
通讯作者：
Stewart,M
中科院分区：
文献类型：
--
作者：
PhillipsJr,GN;Cohen,C;Stewart,M
一种新的晶体形式的原肌球蛋白已经产生，衍射到大约4 Å分辨率。通过缓慢降低精胺的浓度，晶体在室温下生长。这种多胺显然中和了原肌球蛋白的酸性氨基酸侧链，并允许分子紧密并排包装。空间群为C2，胞元尺寸为a= 259.7 a℃，b= 55.3 a℃，c= 135.6 a℃，β= 97.2°。原肌球蛋白分子似乎头尾相连，形成沿着晶体学（332）方向运行的直细丝，其排列与先前描述的薄晶片密切相关。
A new crystalline form of tropomyosin has been produced that diffracts to about 4 Å resolution. The crystals are grown at room temperature by slowly lowering the concentration of spermine. This polyamine apparently neutralizes the acidic amino acid side-chains of tropomyosin and allows close side-by-side packing of molecules. The space group is C2, with unit cell dimensions a= 259.7 A ̊, b= 55.3 A ̊, c= 135.6 A ̊, and β= 97.2°. The tropomyosin molecules appear to be bonded head-to-tail to form straight filaments that run along the crystallographic (332) direction in an arrangement closely related to thin crystalline sheets previously described.