Second virial coefficient:: variations with lysozyme crystallization conditions
Second virial coefficient:: variations with lysozyme crystallization conditions
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DOI：
10.1016/s0022-0248(98)00826-4
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发表时间：
1999-01-01
影响因子：
1.8
通讯作者：
Tardieu, A
中科院分区：
文献类型：
--
作者：
Bonneté, F;Finet, S;Tardieu, A
通过小角X射线散射（SAXS）研究了溶液中溶菌酶颗粒间的相互作用，该相互作用是盐类型（NaCl、NaNO 3、NaSCN和NaOAc）、盐浓度以及温度（30 ℃至10 ℃）的函数。条件的选择涵盖了从（不饱和）溶液到（过饱和）结晶条件的变化。第二维里系数（A（2））由外推到原点的X射线结构因子确定，作为蛋白质浓度的函数。与溶菌酶结晶条件相对应的A（2）值在0 ~-8.0 × 10（-4）mol ml g（-2）范围内，这与其他研究组以前的测定结果一致。第二维里系数从正（排斥相互作用）到负（吸引相互作用）的变化被发现遵循盐诱导结晶的效率。第二维里系数作为预测结晶条件的工具的选择进行了讨论。(C)1999 Elsevier Science B. V.保留所有权利。
Interparticle lysozyme interactions in solution have been studied by small angle X-ray scattering (SAXS) as a function of salt type (NaCl, NaNO3, NaSCN and NaOAc), salt concentration, and as a function of temperature between 30 degrees C and 10 degrees C. The choice of conditions was made to cover variations from (undersaturated) solutions to (supersaturated) crystallization conditions. The second virial coefficients (A(2)) were determined from the X-ray structure factors extrapolated to the origin, as a function of protein concentration. The A(2) values which correspond to lysozyme crystallization conditions were found to be in a range from about zero to -8.0 x 10(-4) mol ml g(-2), in agreement with previous determinations by other groups. The variations of the second virial coefficient from positive (repulsive interactions) to negative (attractive interactions) were found to follow the efficiency of salts to induce crystallization. The choice of the second virial coefficient as a tool to predict crystallization conditions is discussed. (C) 1999 Elsevier Science B.V. All rights reserved.