The experimental determination of the scaling of the superconducting critical temperature ${(T}_c)$ vs the Fermi temperature ${(T}_f)$ of the holes in the boron σ subband is presented. The Fermi level has been tuned near the “shape resonance,” i.e., the two- to three-dimensional crossover of the Fermi surface of the boron σ subband by changing the Al/Mg content in ${\mathrm{Al}}_{1-x}{\mathrm{Mg}}_x{\mathrm{B}}_2.$ The product $k_f{\xi }_0$ of the Fermi wave vector ${(k}_f)$ times the superconducting Pippard coherence length $\left({\xi }_0\right),$ that is a measure of the pairing strength, remains constant, $k_f{\xi }_0=90\mathrm{}$ for $x>\mathrm{}\mathrm{0.66.}\mathrm{}$ This high-$T_c$ phase occurs in the boron superlattice under a tensile microstrain in the range $3\%<\mathrm{}\varepsilon <6\%.\mathrm{}$

Macromolecular X-ray crystallography underpins the vigorous field of structural molecular biology having yielded many protein, nucleic acid and virus structures in fine detail. The understanding of the recognition by these macromolecules, as receptors, of their cognate ligands involves the detailed study of the structural chemistry of their molecular interactions. Also these structural details underpin the rational design of novel inhibitors in modern drug discovery in the pharmaceutical industry. Moreover, from such structures the functional details can be inferred, such as the biological chemistry of enzyme reactivity. There is then a vast number and range of types of biological macromolecules that potentially could be studied. The completion of the protein primary sequencing of the yeast genome, and the human genome sequencing project comprising some 10⁵proteins that is underway, raises expectations for equivalent three dimensional structural databases.