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Crystal structure and molecular modeling of 17-DMAG in complex with human Hsp90.
Crystal structure of the macrocycle-forming thioesterase domain of the erythromycin polyketide synthase: Versatility from a unique substrate channel
- S. Tsai, L. Miercke, R. Stroud
- ChemistryProceedings of the National Academy of Sciences…
- 18 December 2001
As the first structural elucidation of a modular polyketide synthase (PKS) domain, the crystal structure of the macrocycle-forming thioesterase (TE) domain from the 6-deoxyerythronolide B synthase…
Reversed enantioselectivity of diisopropyl fluorophosphatase against organophosphorus nerve agents by rational design.
- M. Melzer, J. Chen, M. Blum
- Chemistry, BiologyJournal of the American Chemical Society
- 6 November 2009
Using the engineered mutants with reversed enantioselectivity and overall enhanced activity against tested nerve agents in combination with wild-type DFPase leads to significantly enhanced activity and detoxification, which is especially important for personal decontamination.
Binding of a designed substrate analogue to diisopropyl fluorophosphatase: implications for the phosphotriesterase mechanism.
- M. Blum, F. Löhr, A. Richardt, H. Rüterjans, J. Chen
- ChemistryJournal of the American Chemical Society
- 7 September 2006
A new mechanism for DFPase activity, which renders the phosphorus atom of the substrate susceptible for attack of water, through generation of a phosphoenzyme intermediate, may be applicable to the structurally related enzyme paraoxonase (PON), a component of high-density lipoprotein (HDL).
Direct observation of hydrogen atom dynamics and interactions by ultrahigh resolution neutron protein crystallography
- J. Chen, B. Hanson, S. Z. Fisher, P. Langan, A. Kovalevsky
- Chemistry, PhysicsProceedings of the National Academy of Sciences
- 4 September 2012
The 1.1 Å, ultrahigh resolution neutron structure of hydrogen/deuterium (H/D) exchanged crambin is reported and has allowed for the anisotropic description of 36 deuterium atoms in the protein.
Seeing the chemistry in biology with neutron crystallography.
- P. Langan, J. Chen
- Chemistry, Materials SciencePhysical chemistry chemical physics : PCCP
- 31 July 2013
Examples of chemistry seen with neutrons for the first time in biological macromolecules over the past few years are described.
Fifteen years of the Protein Crystallography Station: the coming of age of macromolecular neutron crystallography
This article highlights scientific and technical contributions from the Protein Crystallography Station at Los Alamos, the first purpose-built macromolecular crystallography station at a spallation…
Neutron structure and mechanistic studies of diisopropyl fluorophosphatase (DFPase).
- J. Chen, M. Mustyakimov, B. Schoenborn, P. Langan, M. Blum
- Chemistry, BiologyActa crystallographica. Section D, Biological…
- 1 November 2010
A mechanism involving direct nucleophilic attack by Asp229 on the substrate is supported and a mechanism involving metal-assisted water activation is ruled out, enabling the re-engineering of DFPase through rational design to bind and productively orient the more toxic S(P) stereoisomers of the nerve agents sarin and cyclosarin, creating a modified enzyme with enhanced overall activity and significantly increased detoxification properties.
Rapid determination of hydrogen positions and protonation states of diisopropyl fluorophosphatase by joint neutron and X-ray diffraction refinement
- M. Blum, M. Mustyakimov, J. Chen
- ChemistryProceedings of the National Academy of Sciences
- 20 January 2009
Joint refinement has been applied to neutron and X-ray diffraction data collected on crystals of diisopropyl fluorophosphatase (DFPase), a calcium-dependent phosphotriesterase capable of detoxifying organophosphorus nerve agents.
Neutron and Atomic Resolution X-ray Structures of a Lytic Polysaccharide Monooxygenase Reveal Copper-Mediated Dioxygen Binding and Evidence for N-Terminal Deprotonation.
In the neutron and X-ray structures, difference maps reveal the N-terminal amino group, involved in copper coordination, is present as a mixed ND2 and ND-, suggesting a role for the copper ion in shifting the pKa of the amino terminus.