Synthesis and Structural Characterizations of New Coordination Polymers Generated by the Interaction Between the Trinuclear Triangular SBU [Cu 3 (μ 3 -OH)(μ-pz) 3 ] 2+ and 4,4′-Bipyridine. 3°

The reactions of 4,4′-bipyridine with selected trinuclear triangular copper(II) complexes, [Cu3(μ3-OH)(μ-pz)3(RCOO)2Lx], [pz = pyrazolate anion, R = CH3(CH2)n (2 ≤ n ≤ 5); L = H2O, MeOH, EtOH] yielded a series of 1D coordination polymers (CPs) based on the repetition of [Cu3(μ3-OH)(μ-pz)3] secondary building units joined by bipyridine. The CPs were characterized by conventional analytical methods (elemental analyses, ESI-MS, IR spectra) and single crystal XRD determinations. An unprecedented 1D CP, generated through the bipyridine bridging hexanuclear copper clusters moieties, two 1D CPs presenting structural analogies, and two monodimensional tapes having almost exactly superimposable structures, were obtained. In one case, the crystal packing makes evident the presence of small, not-connected pores, accounting for ca. 6% of free cell volume.

Two-Dimensional Crystallisation of Membrane Proteins and Structural Assessment

Two-dimensional (2D) crystallisation of Membrane proteins reconstitutes them into their native environment, the lipid bilayer. Electron crystallography allows the structural analysis of these regular protein–lipid arrays up to atomic resolution. The crystal quality depends on the protein purity, ist stability and on the crystallisation conditions. The basics of 2D crystallisation and different recent advances are reviewed and electron crystallography approaches summarised. Progress in 2D crystallisation, sample preparation, image detectors and automation of the data acquisition and processing pipeline makes 2D electron crystallography particularly attractive for the structural analysis of membrane proteins that are too small for single-particle analyses and too unstable to form three-dimensional (3D) crystals.