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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Nucleation of protein crystals in a wide continuous supersaturation gradient.
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Nucleation of protein crystals in a wide continuous supersaturation gradient.

机译：蛋白质晶体的成核宽连续过度饱和梯度。

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摘要

By using a supersaturation gradient along a protein solution contained in a glass capillary tube, we modified the classical double pulse technique, thus substantially accelerating the procedure of measurement of nucleation parameters. Data for the number of crystal nuclei, n vs nucleation time, t, were obtained for hen-egg-white lysozyme, chosen as a model because of the availability of reliable solubility data in the literature. The stationary nucleation rate and the nucleation time lag have been measured. Quantitative data for the work required for nucleus formation (A(k) = 4.3 x 10 (-1)3 erg) and the size of the critical cluster (three molecules) were also obtained. Besides, it was observed that Ostwald ripening seems to play an important role for nucleation times longer than 150 min. Using the same technique, semi-quantitative investigations were performed with porcine pancreatic trypsin.
机译：通过使用过度饱和梯度沿蛋白质溶液中包含玻璃毛细管管,我们修改了经典的双脉冲技术,从而大大加快成核过程的测量参数。核、n和成核时间t,得到hen-egg-white溶菌酶,被选为一个模型因为可靠的可用性在文献中溶解度数据。成核速度和成核时间滞后被测量。核的形成(所需(k) = 4.3 x 10(1) 3 erg)和集群的大小至关重要(三个分子)也获得了。观察到奥斯特瓦尔德成熟似乎是玩吗成核的重要作用时间更长使用相同的技术,超过150分钟。进行了半定量调查与猪胰腺胰蛋白酶。

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