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#xraycrystallography — Public Fediverse posts

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  1. The first structure of a cold-active arginase reveals a modest reduction in structural rigidity associated with cold adaptation @BirkbeckUoL @ActaCrystF @IUCr #ColdActiveEnzymes #Arginases #XRayCrystallography doi.org/10.1107/S2053230X26003

  2. The first structure of a cold-active arginase reveals a modest reduction in structural rigidity associated with cold adaptation @BirkbeckUoL @ActaCrystF @IUCr #ColdActiveEnzymes #Arginases #XRayCrystallography doi.org/10.1107/S2053230X26003

  3. The first structure of a cold-active arginase reveals a modest reduction in structural rigidity associated with cold adaptation @BirkbeckUoL @ActaCrystF @IUCr #ColdActiveEnzymes #Arginases #XRayCrystallography doi.org/10.1107/S2053230X26003

  4. Modifying the bacterial strain led to cleaner bacterial expression of a synthetic BRIL antibody that facilitates protein structure determination via both crystallography and cryo-EM #CryoEM #XRayCrystallography #BRIL doi.org/10.1107/S2053230X26001

  5. Modifying the bacterial strain led to cleaner bacterial expression of a synthetic BRIL antibody that facilitates protein structure determination via both crystallography and cryo-EM #CryoEM #XRayCrystallography #BRIL doi.org/10.1107/S2053230X26001

  6. Modifying the bacterial strain led to cleaner bacterial expression of a synthetic BRIL antibody that facilitates protein structure determination via both crystallography and cryo-EM #CryoEM #XRayCrystallography #BRIL doi.org/10.1107/S2053230X26001

  7. High-resolution structures of α-bCA2 with sulfonamide derivatives provides experimentally supported information defining their binding mode and supporting inhibitor optimization #CarbonicAnhydraseII #SulfonamideInhibitors #XRayCrystallography doi.org/10.1107/S2053230X26002

  8. High-resolution structures of α-bCA2 with sulfonamide derivatives provides experimentally supported information defining their binding mode and supporting inhibitor optimization #CarbonicAnhydraseII #SulfonamideInhibitors #XRayCrystallography doi.org/10.1107/S2053230X26002

  9. High-resolution structures of α-bCA2 with sulfonamide derivatives provides experimentally supported information defining their binding mode and supporting inhibitor optimization #CarbonicAnhydraseII #SulfonamideInhibitors #XRayCrystallography doi.org/10.1107/S2053230X26002

  10. How do enzymes, nature's highly efficient catalysts, achieve almost perfect precision and efficiency?

    This is the research question to be addressed by newly funded project in chemistry: “NEXT - Quantum Biology”. The funding will strengthen #interdisciplinary teams and bridge #StructureBiology and #QuantumPhysics.

    Congratulations to researchers at our Uni, MPI-NAT in Göttingen, and Hamburg Uni: www.uni-goettingen.de/en/3240.html?id=8028. With thanks to the Volkswagen Foundation.

    #Chemistry #QuantumBiology #XrayCrystallography

  11. How do enzymes, nature's highly efficient catalysts, achieve almost perfect precision and efficiency?

    This is the research question to be addressed by newly funded project in chemistry: “NEXT - Quantum Biology”. The funding will strengthen #interdisciplinary teams and bridge #StructureBiology and #QuantumPhysics.

    Congratulations to researchers at our Uni, MPI-NAT in Göttingen, and Hamburg Uni: www.uni-goettingen.de/en/3240.html?id=8028. With thanks to the Volkswagen Foundation.

    #Chemistry #QuantumBiology #XrayCrystallography

  12. How do enzymes, nature's highly efficient catalysts, achieve almost perfect precision and efficiency?

    This is the research question to be addressed by newly funded project in chemistry: “NEXT - Quantum Biology”. The funding will strengthen #interdisciplinary teams and bridge #StructureBiology and #QuantumPhysics.

    Congratulations to researchers at our Uni, MPI-NAT in Göttingen, and Hamburg Uni: www.uni-goettingen.de/en/3240.html?id=8028. With thanks to the Volkswagen Foundation.

    #Chemistry #QuantumBiology #XrayCrystallography

  13. How do enzymes, nature's highly efficient catalysts, achieve almost perfect precision and efficiency?

    This is the research question to be addressed by newly funded project in chemistry: “NEXT - Quantum Biology”. The funding will strengthen #interdisciplinary teams and bridge #StructureBiology and #QuantumPhysics.

    Congratulations to researchers at our Uni, MPI-NAT in Göttingen, and Hamburg Uni: www.uni-goettingen.de/en/3240.html?id=8028. With thanks to the Volkswagen Foundation.

    #Chemistry #QuantumBiology #XrayCrystallography

  14. How do enzymes, nature's highly efficient catalysts, achieve almost perfect precision and efficiency?

    This is the research question to be addressed by newly funded project in chemistry: “NEXT - Quantum Biology”. The funding will strengthen #interdisciplinary teams and bridge #StructureBiology and #QuantumPhysics.

    Congratulations to researchers at our Uni, MPI-NAT in Göttingen, and Hamburg Uni: www.uni-goettingen.de/en/3240.html?id=8028. With thanks to the Volkswagen Foundation.

    #Chemistry #QuantumBiology #XrayCrystallography

  15. Features of sample preparation that should be considered prior to biomolecular crystallization experiments are reviewed, as described in the SAMPREP workshop during the 73rd Annual ACA Meeting #Crystallization #XRayCrystallography #StructuralBiology doi.org/10.1107/S2053230X25004

  16. Features of sample preparation that should be considered prior to biomolecular crystallization experiments are reviewed, as described in the SAMPREP workshop during the 73rd Annual ACA Meeting #Crystallization #XRayCrystallography #StructuralBiology doi.org/10.1107/S2053230X25004

  17. Features of sample preparation that should be considered prior to biomolecular crystallization experiments are reviewed, as described in the SAMPREP workshop during the 73rd Annual ACA Meeting #Crystallization #XRayCrystallography #StructuralBiology doi.org/10.1107/S2053230X25004

  18. The structure of the C1 domain of the surface-layer protein SlpM from L. brevis provides new insights into the architecture and evolutionary adaptability of SLPs in Lactobacillus species #XRayCrystallography #SurfaceLayerProtein #SlpM doi.org/10.1107/S2053230X25004

  19. The structure of the C1 domain of the surface-layer protein SlpM from L. brevis provides new insights into the architecture and evolutionary adaptability of SLPs in Lactobacillus species #XRayCrystallography #SurfaceLayerProtein #SlpM doi.org/10.1107/S2053230X25004

  20. The structure of the C1 domain of the surface-layer protein SlpM from L. brevis provides new insights into the architecture and evolutionary adaptability of SLPs in Lactobacillus species #XRayCrystallography #SurfaceLayerProtein #SlpM doi.org/10.1107/S2053230X25004

  21. Unlike other serpins, human serpin B9 shows significant structural deviations around helix D, with a larger surface cavity, which could serve as a promising target for small-molecule inhibitors #Serpins #XRayCrystallography #Crystallization t.co/ilB7Aa3Krg

  22. Unlike other serpins, human serpin B9 shows significant structural deviations around helix D, with a larger surface cavity, which could serve as a promising target for small-molecule inhibitors #Serpins #XRayCrystallography #Crystallization t.co/ilB7Aa3Krg

  23. Unlike other serpins, human serpin B9 shows significant structural deviations around helix D, with a larger surface cavity, which could serve as a promising target for small-molecule inhibitors #Serpins #XRayCrystallography #Crystallization t.co/ilB7Aa3Krg

  24. The structure of the Rib domain from Limosilactobacillus reuteri is compared with previously published models and is found to exhibit extraordinary thermal stability #XRayCrystallography #RibDomain #ImmunoglobulinLikeFold t.co/y4cUSd1bHR

  25. The structure of the Rib domain from Limosilactobacillus reuteri is compared with previously published models and is found to exhibit extraordinary thermal stability #XRayCrystallography #RibDomain #ImmunoglobulinLikeFold t.co/y4cUSd1bHR

  26. The structure of the Rib domain from Limosilactobacillus reuteri is compared with previously published models and is found to exhibit extraordinary thermal stability #XRayCrystallography #RibDomain #ImmunoglobulinLikeFold t.co/y4cUSd1bHR

  27. A true apo PTPN2 crystal structure with an unbound active site allowed the active site to be observed in a native apo state for the first time and inhibitor complexes were obtained by soaking experiments #PTPN2 #Phosphatases #XRayCrystallography doi.org/10.1107/S2053230X24007

  28. A true apo PTPN2 crystal structure with an unbound active site allowed the active site to be observed in a native apo state for the first time and inhibitor complexes were obtained by soaking experiments #PTPN2 #Phosphatases #XRayCrystallography doi.org/10.1107/S2053230X24007

  29. A true apo PTPN2 crystal structure with an unbound active site allowed the active site to be observed in a native apo state for the first time and inhibitor complexes were obtained by soaking experiments #PTPN2 #Phosphatases #XRayCrystallography doi.org/10.1107/S2053230X24007

  30. This long Rib domain demonstrates a highly conserved structure and also highlights an evolutionary convergence in structural architecture with other modular domains in cell-adhesion molecules. #BacterialAdhesins #RibDomains #XRayCrystallography t.co/NxObHw6qHN

  31. This long Rib domain demonstrates a highly conserved structure and also highlights an evolutionary convergence in structural architecture with other modular domains in cell-adhesion molecules. #BacterialAdhesins #RibDomains #XRayCrystallography t.co/NxObHw6qHN

  32. This long Rib domain demonstrates a highly conserved structure and also highlights an evolutionary convergence in structural architecture with other modular domains in cell-adhesion molecules. #BacterialAdhesins #RibDomains #XRayCrystallography t.co/NxObHw6qHN

  33. SBGrid's eLife paper received a new citation in August from SBGrid member Stephen Blacklow Harvard Medical School in Cell: Structural basis for membrane-proximal proteolysis of substrates by ADAM10.

    Read more at: cell.com/cell/pdf/S0092-8674(2

    <ALT= Structural Basis for Regulated Proteolysis by the α-Secretase ADAM10>

    #SBGrid #publications #Science #xraycrystallography #ADAM10

  34. SBGrid's eLife paper received a new citation in August from SBGrid member Stephen Blacklow Harvard Medical School in Cell: Structural basis for membrane-proximal proteolysis of substrates by ADAM10.

    Read more at: cell.com/cell/pdf/S0092-8674(2

    <ALT= Structural Basis for Regulated Proteolysis by the α-Secretase ADAM10>

    #SBGrid #publications #Science #xraycrystallography #ADAM10

  35. The first serial synchrotron crystallography structure of apo PTP1B indicates a degree of allosteric decoupling that adds nuance to the previously reported paradigm of allostery in this protein #XRayCrystallography #Phosphatase #Allostery #openaccess doi.org/10.1107/S2053230X22011

  36. The first serial synchrotron crystallography structure of apo PTP1B indicates a degree of allosteric decoupling that adds nuance to the previously reported paradigm of allostery in this protein #XRayCrystallography #Phosphatase #Allostery #openaccess doi.org/10.1107/S2053230X22011

  37. Hi @DNPFred
    In grad school I worked on heme proteins using #paramagnetic #NMR and #NRVS. Then I shifted to #XRayCrystallography, using #EPR #UVVis and #EDX on #crystals when a postdoc. My research group works on #NonHemeIron #enzymes, & #heme, #copper & #manganese #metalloproteins. Really interested in combining #spectroscopy on #protein #crystals to examine #structure #function relationships.