Novel approach to controlled protein crystallization through ligandation of yttrium cations
Novel approach to controlled protein crystallization through ligandation of yttrium cations
复制标题
通过钇阳离子配体控制蛋白质结晶的新方法
DOI:
--
复制
发表时间:
2011
期刊:
影响因子:
--
通讯作者:
F. Schreiber
中科院分区:
文献类型:
--
作者:
Fajun Zhang;G. Zocher;A. Sauter;T. Stehle;F. Schreiber
Crystal structure determination of macromolecules is often hampered by the lack of crystals suitable for diffraction experiments. This article describes a protocol to crystallize the acidic protein bovine β-lactoglobulin in the presence of yttrium to yield high-quality crystals that belong to a new space group. The yttrium ions not only are used to engineer the crystallization, but are an integral part of the crystal lattice and can therefore be used to solve the phase problem using anomalous dispersion methods. Protein crystallization conditions were first optimized using an experimental phase diagram in the protein and salt concentration plane. Crystal growth strongly depends on the position in the phase diagram, and the best crystals grow near the phase transition boundaries. The structure analysis demonstrates the specific binding of yttrium ions to surface-exposed glutamate and aspartate side chains contributed by different molecules in the crystal lattice. By bridging molecules in this manner, contacts between molecules are formed that enable the formation of a stable crystal lattice. The potential application of this strategy to the crystallization of other acidic proteins is discussed on the basis of the universal features of the phase behavior of these proteins and the interactions induced by multivalent ions.
影响因子:
4.2
作者:
P. Adams;K. Gopal;R. Grosse-Kunstleve;L. Hung;T. Ioerger;A. Mccoy;N. Moriarty;Reetal Pai;
通讯作者:
P. Adams;K. Gopal;R. Grosse-Kunstleve;L. Hung;T. Ioerger;A. Mccoy;N. Moriarty;Reetal Pai;
DOI:
10.1073/pnas.0507591102
发表时间:
2005-10-18
影响因子:
11.1
作者:
Bouyain, S;Longo, PA;Leahy, DJ
通讯作者:
Leahy, DJ