A set of three-dimensional charge-density-wave (3D CDW) VSe2 nano-flakes with different thicknesses were obtained by the scotch tape-based micro-mechanical exfoliation method. Resistivity measurements showed that the 3D CDW transition temperature Tp decreases systematically from 105 K in bulk to 81.8 K in the 11.6 nm thick flake. The Hall resistivity ρxy of all the flakes showed a linear dependent behavior against the magnetic field with a residual electron concentration of the order of ∼1021 cm−3 at 5 K. The electron concentration n increases slightly as the thickness d decreases, possibly due to the CDW gap is reduced with the decrease of the thickness.

Two crystal structures of the C123S mutant of 2-methylisocitrate lyase have been determined, one with the bound reaction products, Mg(2+)-pyruvate and succinate, and the second with a bound Mg(2+)-(2R,3S)-isocitrate inhibitor. Comparison with the structure of the wild-type enzyme in the unbound state reveals that the enzyme undergoes a conformational transition that sequesters the ligand from solvent, as previously observed for two other enzyme superfamily members, isocitrate lyase and phosphoenolpyruvate mutase. The binding modes reveal the determinants of substrate specificity and stereoselectivity, and the stringent specificity is verified in solution using various potential substrates. A model of bound 2-methylisocitrate has been developed based on the experimentally determined structures. We propose a catalytic mechanism involving an alpha-carboxy-carbanion intermediate/transition state, which is consistent with previous stereochemical experiments showing inversion of configuration at the C(3) of 2-methylisocitrate. Structure-based sequence analysis and phylogenic tree construction reveal determinants of substrate specificity, highlight nodes of divergence of families, and predict enzyme families with new functions.