Crystallization and preliminary X-ray diffraction studies of a 40 kDa calcium binding protein specifically expressed in plasmodia of Physarum polycephalum.
Crystallization and preliminary X-ray diffraction studies of a 40 kDa calcium binding protein specifically expressed in plasmodia of Physarum polycephalum.
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在多头绒泡菌疟原虫中特异性表达的 40 kDa 钙结合蛋白的结晶和初步 X 射线衍射研究。
DOI：
10.1093/oxfordjournals.jbchem.a022438
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发表时间：
1999
影响因子：
2.7
通讯作者：
M. Tanokura
中科院分区：
文献类型：
--
作者：
W. Iwasaki;H. Sasaki;A. Nakamura;K. Kohama;M. Tanokura
在EDTA的作用下，多头绒泡菌（Physarum polycephalum）疟原虫特异性LAV1-2基因产物钙结合蛋白（CBP40）的分子量为40 kDa。这些晶体衍射x射线的分辨率可达3.0安。它们属于三角形空间群P3221（或P3121），单位胞尺寸为a = b = 64.4 a, c = 207.2 a。通过在CaCl2溶液中浸泡得到Ca2+结合晶体，得到了类似质量的衍射数据。Ca2+浸泡晶体与EDTA存在下结晶的晶体属于同一空间群，单位胞尺寸分别为a = b = 64.4 a和c = 209.4 a。
A calcium binding protein with a molecular mass of 40 kDa (CBP40), the gene product of plasmodial-specific LAV1-2 of Physarum polycephalum, was crystallized in the presence of EDTA. The crystals diffracted X-rays up to a resolution of 3.0 A. They belonged to the trigonal space group, P3221 (or P3121), with unit cell dimensions of a = b = 64.4 A and c = 207.2 A. Ca2+-bound crystals were obtained by soaking in a CaCl2 solution, which gave diffraction data of similar quality. The Ca2+-soaked crystals belonged to the same space group as those crystallized in the presence of EDTA with unit cell dimensions of a = b = 64.4 A and c = 209.4 A.