5MF2

Bacteriophage T5 distal tail protein pb9 co-crystallized with Tb-Xo4

Summary for 5MF2

• Entry DOI: 10.2210/pdb5mf2/pdb
• Descriptor: Distal tail protein, TERBIUM(III) ION, Tb-Xo4, ... (5 entities in total)
• Functional Keywords: lanthanide complexes, crystallogenesis, anomalous scattering, bacteriophages, viral protein
• Biological source: Escherichia phage T5
• Total number of polymer chains: 4
• Total formula weight: 101635.68

Authors

Engilberge, S.,Riobe, F.,Di Pietro, S.,Lassalle, L.,Arnaud, C.-A.,Breyton, C.,Madern, D.,Coquelle, N.,Maury, O.,Girard, E. (deposition date: 2016-11-17, release date: 2017-09-20, Last modification date: 2024-05-08)

Primary citation

Engilberge, S.,Riobe, F.,Di Pietro, S.,Lassalle, L.,Coquelle, N.,Arnaud, C.A.,Pitrat, D.,Mulatier, J.C.,Madern, D.,Breyton, C.,Maury, O.,Girard, E.
Crystallophore: a versatile lanthanide complex for protein crystallography combining nucleating effects, phasing properties, and luminescence.
Chem Sci, 8:5909-5917, 2017

PubMed Abstract: Macromolecular 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.

PubMed: 29619195
DOI: 10.1039/c7sc00758b

Experimental method

X-RAY DIFFRACTION (2 Å)