Crystallizatioin and preliminary X-ray analysis of a putative sensor histidine kinase domain : the C-terminal domain of HksP4 from Aquifex aecolicus VF5
Crystallizatioin and preliminary X-ray analysis of a putative sensor histidine kinase domain : the C-terminal domain of HksP4 from Aquifex aecolicus VF5
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假定的传感器组氨酸激酶结构域的结晶和初步 X 射线分析：来自 Aquifex aecolicus VF5 的 HksP4 的 C 末端结构域
DOI：
10.1107/s1744309111018434
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发表时间：
2011
期刊：
影响因子：
--
通讯作者：
M.Tanokura
中科院分区：
文献类型：
--
作者：
S.Horita;Y.Yamanaka;A.Yamamura;A.Okada;J.Nakayama,K.Nagata;M.Tanokura
表达、纯化和结晶了来自超嗜热菌风产液菌VF 5的胞质蛋白HksP 4的组氨酸激酶结构域，该结构域位于蛋白质的C-末端的一半。以聚乙二醇3350为沉淀剂，在三磷酸腺苷（ATP）或5′-（β，γ-亚氨基）三磷酸腺苷（AMPPNP）存在下，采用坐滴气相扩散法获得了衍射级晶体。在ATP和AMPPNP存在下获得的晶体在Photon Factory（茨木，日本）的BL-5A上分别衍射X射线至3.1和2.9 μ m分辨率，并且被发现属于相同的空间群P212121，晶胞参数分别为a = 80.2，B = 105.5，c = 122.0 μ m和a = 81.5，B = 105.5，c = 130.9 μ m。 它们的马修斯系数（VM分别为2.74和2.51 3 Da−1）表明，两种晶体的每个不对称单位都含有4个蛋白质分子。
The histidine kinase domain of the cytoplasmic protein HksP4 from the hyperthermophilic bacterium Aquifex aeolicus VF5, located in the C-terminal half of the protein, was expressed, purified and crystallized. Diffraction-quality crystals were obtained in the presence of adenosine triphosphate (ATP) or adenosine 5′-(β,γ-imido)triphosphate (AMPPNP) by the sitting-drop vapour-diffusion method using PEG 3350 as the precipitant. The crystals obtained in the presence of ATP and AMPPNP diffracted X-rays to 3.1 and 2.9 Å resolution, respectively, on BL-5A at Photon Factory (Ibaraki, Japan) and were found to belong to the same space group P212121, with unit-cell parameters a = 80.2, b = 105.5, c = 122.0 Å and a = 81.5, b = 105.5, c = 130.9 Å, respectively. Their Matthews coefficients (VM = 2.74 and 2.51 Å3 Da−1, respectively) indicated that both crystals contained four protein molecules per asymmetric unit.