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Protein conformational relaxation and ligand migration in myoglobin: a nanosecond to millisecond molecular movie from time-resolved Laue X-ray diffraction.
These results demonstrate that structural changes as small as 0.2 A and populations of CO docking sites of 10% can be detected by time-resolved X-ray diffraction. Expand
Structural basis of enhanced photoconversion yield in green fluorescent protein-like protein Dendra2.
The structure, which is very similar to those reported for the closely related proteins EosFP and Kaede, revealed a local structural change involving mainly Arg66 and a water molecule W4, which are part of a charged and hydrogen-bonded cluster of amino acids and water molecules next to the chromophore. Expand
Photolysis of the Carbon Monoxide Complex of Myoglobin: Nanosecond Time-Resolved Crystallography
Time-resolving experiments reveal the structures of myoglobin photoproducts, provide a structural foundation to spectroscopic results and molecular dynamics calculations, and demonstrate that time-resolved macromolecular crystallography can elucidate the structural bases of biochemical mechanisms on the nanosecond time scale. Expand
Complex landscape of protein structural dynamics unveiled by nanosecond Laue crystallography
It is proposed that the extended relaxation of the globin moiety reflects reequilibration among conformational substates known to play an essential role in controlling protein function. Expand
Structural characterization of IrisFP, an optical highlighter undergoing multiple photo-induced transformations
Crystallography and spectroscopy are combined to characterize the Phe-173-Ser mutant of the tetrameric variant of EosFP, named IrisFP, which incorporates both types of phototransformations and displays altogether 3 distinct photoactivation processes. Expand
Structural basis for the phototoxicity of the fluorescent protein KillerRed
The presence of a partially mature, photo‐resistant, green‐emitting state is characterized, which accounts for enhanced CALI by “pre‐bleached” KillerRed, and mechanisms for ROS production and self protection are proposed. Expand
The crystal structure of a llama heavy chain variable domain
The 1.85 Å structure of an antigen-free llama heavy chain variable domain reveals a fold similarity to that of the classical immunoglobulin VHs, increased surface hydrophilicity of the side of the VHExpand
Advances in kinetic protein crystallography.
Laue diffraction has now reached an unprecedented level of sophistication and has found a 'niche of excellence' in the study of cyclic, ultra-fast, light-triggered reactions. Expand
Extended subnanosecond structural dynamics of myoglobin revealed by Laue crystallography.
Subnanosecond time-resolved Laue diffraction data on the triple mutant YQR-Mb depict the sequence of structural events associated with heme and protein relaxation from 100 ps to 316 ns and above, suggesting that the internal structure controls the rate and amplitude of the relaxation events. Expand
N-terminal arm exchange is observed in the 2.15 A crystal structure of oxidized nitrite reductase from Pseudomonas aeruginosa.
The unexpected domain-crossing by the N-terminal segment of NiR-Pa is comparable to that of 'domain swapping' or 'arm exchange' previously observed in other systems and may explain the observed cooperativity between monomers of dimeric NiR -Pa. Expand