5mf2
From Proteopedia
Bacteriophage T5 distal tail protein pb9 co-crystallized with Tb-Xo4
Structural highlights
FunctionDIT_BPT5 Distal tail protein which forms a hexameric ring located at the tail tube end.[1] Publication Abstract from PubMedMacromolecular crystallography suffers from two major issues: getting well-diffracting crystals and solving the phase problem inherent to large macromolecules. Here, we describe the first example of a lanthanide complex family named "crystallophore" (Xo4), which contributes to tackling both bottlenecks. This terbium complex, Tb-Xo4, is an appealing agent for biocrystallography, combining the exceptional phasing power of the Tb(iii) heavy atom with powerful nucleating properties, providing ready-to-use crystals for structure determination. Furthermore, protein/Tb-Xo4 co-crystals can be easily detected and discriminated from other crystalline by-products using luminescence. We demonstrate the potential of this additive for the crystallisation and structure determination of eight proteins, two of whose structures were unknown. Crystallophore: a versatile lanthanide complex for protein crystallography combining nucleating effects, phasing properties, and luminescence.,Engilberge S, Riobe F, Di Pietro S, Lassalle L, Coquelle N, Arnaud CA, Pitrat D, Mulatier JC, Madern D, Breyton C, Maury O, Girard E Chem Sci. 2017 Sep 1;8(9):5909-5917. doi: 10.1039/c7sc00758b. Epub 2017 Jun 6. PMID:29619195[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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Categories: Escherichia virus T5 | Large Structures | Arnaud C-A | Breyton C | Coquelle N | Di Pietro S | Engilberge S | Girard E | Lassalle L | Madern D | Maury O | Riobe F
