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A genetically-encoded photoactivatable Rac controls the motility of living cells
A new approach to produce genetically encoded photoactivatable derivatives of Rac1, a key GTPase regulating actin cytoskeletal dynamics in metazoan cells, which was shown to inhibit RhoA in mouse embryonic fibroblasts, with inhibition modulated at protrusions and ruffles. Expand
Structure and chemistry of cytochrome P450.
This review will concentrate on findings with P-450cam of the Pseudomonas putida camphor-5-exo-hydroxylase, and attention will be drawn to parallel and contrasting examples from other P- 450s as appropriate. Expand
Femtosecond X-ray protein nanocrystallography
This work offers a new approach to structure determination of macromolecules that do not yield crystals of sufficient size for studies using conventional radiation sources or are particularly sensitive to radiation damage, by using pulses briefer than the timescale of most damage processes. Expand
The catalytic pathway of cytochrome p450cam at atomic resolution.
Structures were obtained for three intermediates in the hydroxylation reaction of camphor by P450cam with trapping techniques and cryocrystallography and reveal a network of bound water molecules that may provide the protons needed for the reaction. Expand
Structure and mechanism of a bacterial light-regulated cyclic nucleotide phosphodiesterase
Crystal structures of BlrP1 complexed with its substrate and metal ions involved in catalysis or in enzyme inhibition provide a detailed understanding of the mechanism of the EAL-domain c-di-GMP phosphodiesterase output activity. Expand
Crystal structures of myoglobin-ligand complexes at near-atomic resolution.
We have used x-ray crystallography to determine the structures of sperm whale myoglobin (Mb) in four different ligation states (unligated, ferric aquomet, oxygenated, and carbonmonoxygenated) to aExpand
Crystal structure of photolysed carbonmonoxy-myoglobin
X-ray crystallography at liquid-helium temperatures is used to determine the structure of Mb*CO to a resolution of 1.5 Å and reveals that on photodissociation of the CO, the haem 'domes', the iron moves partially out of the haems plane, the iron–proximal histidine bond is compressed, the F helix is strained and the distal histidine swings towards the outside of the ligand-binding pocket. Expand
Kinetic and structural analysis of the Mg(2+)-binding site of the guanine nucleotide-binding protein p21H-ras.
P NMR spectra of the GDP and Gpp(NH)p (guanosine-5'-(beta,gamma-imido)triphosphate) complexes of mutated p21 show a remarkable perturbation of the guanine nucleotide-binding site compared to wild-type protein. Expand
High-Resolution Protein Structure Determination by Serial Femtosecond Crystallography
Serial femtosecond crystallography (SFX) is applied using an x-ray free-electron laser (XFEL) to obtain high-resolution structural information from microcrystals of the well-characterized model protein lysozyme, demonstrating the immediate relevance of SFX for analyzing the structure of the large group of difficult-to-crystallize molecules. Expand
The bottleneck in AZT activation
Determination of the structure of thymidylate kinase as a complex with AZT monophosphate (AZTMP) together with studies on the kinetics of its phosphorylation have now led to a detailed understanding of the reasons for and consequences of the poor substrate properties. Expand