Erratum: Publisher's Note: "Enzyme transient state kinetics in crystal and solution from the perspective of a time-resolved crystallographer" [Struct. Dyn. , 024701 (2014)].

[This corrects the article DOI: 10.1063/1.4869472.

Enhanced hydrogenation activity and diastereomeric interactions of methyl pyruvate co-adsorbed with R-1-(1-naphthyl)ethylamine on Pd(111).

Unmodified racemic sites on heterogeneous chiral catalysts reduce their overall enantioselectivity, but this effect is mitigated in the Orito reaction (methyl pyruvate (MP) hydrogenation to methyl lactate) by an increased hydrogenation reactivity. Here, this effect is explored on a R-1-(1-naphthyl)ethylamine (NEA)-modified Pd(111) model catalyst where temperature-programmed desorption experiments reveal that NEA accelerates the rates of both MP hydrogenation and H/D exchange. NEA+MP docking complexes are imaged using scanning tunnelling microscopy supplemented by density functional theory calculations to allow the most stable docking complexes to be identified.

Enzyme transient state kinetics in crystal and solution from the perspective of a time-resolved crystallographer.

With recent technological advances at synchrotrons [Graber et al., J. Synchrotron Radiat.

Three-dimensional single-particle imaging using angular correlations from X-ray laser data.

Femtosecond X-ray pulses from X-ray free-electron laser sources make it feasible to conduct room-temperature solution scattering experiments far below molecular rotational diffusion timescales. Owing to the ultra-short duration of each snapshot in these fluctuation scattering experiments, the particles are effectively frozen in space during the X-ray exposure. In contrast to standard small-angle scattering experiments, the resulting scattering patterns are anisotropic.