Lorber B, Sauter C, Robert M C, Capelle B, Giegé R
UPR 9002, Institut de Biologie Moléculaire et Cellulaire du CNRS, 15 Rue René Descartes, 67084 Strasbourg CEDEX, France.
Acta Crystallogr D Biol Crystallogr. 1999 Sep;55(Pt 9):1491-4. doi: 10.1107/s0907444999008902.
To prevent crystals from moving in orbit and sedimenting upon their return to earth, the model protein thaumatin was crystallized in agarose gel in the Advanced Protein Crystallization Facility during the eight-day Space Shuttle mission STS-95 (November 1998). The quality of tetragonal crystals grown in microgravity was compared with that of controls prepared in parallel in the laboratory. On the basis of their diffraction properties, microgravity crystals were more ordered than crystals grown in gel on earth (the latter being, on average, better than reference crystals obtained in solution on earth). It is concluded that protein crystallization within a gel in microgravity may yield crystals of superior quality by combining the advantages of both environments. A possible explanation for the positive effect of microgravity on protein crystallization in gels involving the better quality of the nucleus is discussed.
为防止晶体在轨道上移动并在返回地球时沉降，在1998年11月为期八天的航天飞机任务STS - 95期间，在先进蛋白质结晶设施中，模型蛋白奇异果甜蛋白在琼脂糖凝胶中进行了结晶。将在微重力下生长的四方晶体的质量与在实验室中平行制备的对照晶体的质量进行了比较。基于它们的衍射特性，微重力晶体比在地球上凝胶中生长的晶体更有序（后者平均而言优于在地球上溶液中获得的参比晶体）。得出的结论是，微重力下凝胶内的蛋白质结晶可能通过结合两种环境的优点产生质量更高的晶体。讨论了微重力对凝胶中蛋白质结晶产生积极影响的一种可能解释，该解释涉及晶核的更好质量。
