Carey J. Kassmann

TL;DR: The 1.30 A resolution crystal structure of nickel superoxide dismutase (NiSOD) identifies a novel SOD fold, assembly, and Ni active site that provides almost all interactions critical for metal binding and catalysis, and thus will likely be diagnostic of NiSODs.

TL;DR: Characterizations of beta-barrel (H43R) and dimer interface (A4V) FALS mutants reveal reduced stability and drastically increased aggregation propensity, and electron and atomic force microscopy indicate that these defects promote the formation of filamentous aggregates.

TL;DR: The protein architecture contains a dramatic ≈80° bend in the central helix, which focuses distortions at G67 to promote ring formation from amino acids S65, Y66, and G67, and this leads directly to a conjugation-trapping mechanism, in which a thermodynamically unfavorable cyclization reaction is coupled to an electronic conjugations trapping step, to drive chromophore maturation.

TL;DR: High-resolution structures reveal how structure-based design has effectively linked selective metal binding to changes in fluorescent properties and provides a prototype suitable for further optimization by directed evolution to generate metalloprotein variants with desirable physical or biochemical properties.

TL;DR: The Aequorea victoria green fluorescent protein (GFP) undergoes a remarkable post-translational modification to create a chromophore out of its component amino acids S65, Y66, and G67.