Gorrec Fabrice, Bellini Dom
Structural Studies, MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, Cambridgeshire CB2 0QH, United Kingdom.
J Appl Crystallogr. 2022 Mar 11;55(Pt 2):310-319. doi: 10.1107/S1600576722001765. eCollection 2022 Apr 1.
The success and speed of atomic structure determination of biological macromolecules by X-ray crystallography depends critically on the availability of diffraction-quality crystals. However, the process of screening crystallization conditions often consumes large amounts of sample and time. An innovative protein crystallization screen formulation called FUSION has been developed to help with the production of useful crystals. The concept behind the formulation of FUSION was to combine the most efficient components from the three MORPHEUS screens into a single screen using a systematic approach. The resulting formulation integrates 96 unique combinations of crystallization additives. Most of these additives are small molecules and ions frequently found in crystal structures of the Protein Data Bank (PDB), where they bind proteins and complexes. The efficiency of FUSION is demonstrated by obtaining high yields of diffraction-quality crystals for seven different test proteins. In the process, two crystal forms not currently in the PDB for the proteins α-amylase and avidin were discovered.
通过X射线晶体学确定生物大分子原子结构的成功与速度，严重依赖于具有衍射质量的晶体的可得性。然而，筛选结晶条件的过程常常消耗大量样品和时间。一种名为FUSION的创新性蛋白质结晶筛选配方已被开发出来，以助力有用晶体的生产。FUSION配方背后的理念是使用系统方法，将来自三个MORPHEUS筛选中的最有效成分组合到一个单一筛选中。所得配方整合了96种独特的结晶添加剂组合。这些添加剂大多是在蛋白质数据库（PDB）的晶体结构中经常发现的小分子和离子，它们在其中与蛋白质及复合物结合。通过为七种不同的测试蛋白获得高产率的具有衍射质量的晶体，证明了FUSION的效率。在此过程中，发现了蛋白质α-淀粉酶和抗生物素蛋白目前在PDB中尚未有的两种晶体形式。
