Flores-Hernández Edith, Stojanoff Vivian, Arreguín-Espinosa Roberto, Moreno Abel, Sánchez-Puig Nuria
Departamento de Química de Biomacromoléculas, Instituto de Química, Universidad Nacional Autónoma de México, Avenida Universidad 3000, Ciudad Universitaria, CP 04510, México, DF, México.
J Appl Crystallogr. 2013 Jun 1;46(Pt 3):832-834. doi: 10.1107/S0021889813010558. Epub 2013 May 15.
A new easy-to-use device has been designed and implemented for electric field-induced protein crystallization in a vapor-diffusion configuration. The device not only controls crystal nucleation by means of the electrical current, but also favors crystal growth owing to its vapor-diffusion setup. Crystallization was conducted in the presence of an internal electric field and direct current. The proteins investigated were lysozyme, as model protein, and 2TEL-lysozyme (a synthetic protein consisting of two tandem alpha helix motifs connected to a lysozyme moiety). Lysozyme crystals that grew attached to the cathode were larger than those grown attached to the anode or in the absence of an electric current. On the other hand, crystals of 2TEL-lysozyme qualitatively showed a better X-ray diffraction pattern when grown in the presence of an electric current.
一种新型的易于使用的装置已被设计并应用于蒸汽扩散配置下的电场诱导蛋白质结晶。该装置不仅通过电流控制晶体成核,还因其蒸汽扩散设置有利于晶体生长。结晶是在内部电场和直流电存在的情况下进行的。所研究的蛋白质是作为模型蛋白质的溶菌酶以及2TEL-溶菌酶(一种由两个串联的α螺旋基序连接到溶菌酶部分组成的合成蛋白质)。附着在阴极生长的溶菌酶晶体比附着在阳极生长的或在无电流情况下生长的晶体更大。另一方面,2TEL-溶菌酶晶体在有电流存在的情况下生长时,定性地显示出更好的X射线衍射图谱。