Charge-density analysis of an iron-sulfur protein at an ultra-high resolution of 0.48 Å.
about
How cryo-electron microscopy and X-ray crystallography complement each other.Crystallographic characterization of the high-potential iron-sulfur protein in the oxidized state at 0.8 Å resolution.Distribution of valence electrons of the flavin cofactor in NADH-cytochrome b5 reductase.Fifteen years of the Protein Crystallography Station: the coming of age of macromolecular neutron crystallography.Role of water and protein dynamics in proton pumping by respiratory complex I.Influences of lone-pair electrons on directionality of hydrogen bonds formed by hydrophilic amino acid side chains in molecular dynamics simulation.Sub-ångström cryo-EM structure of a prion protofibril reveals a polar clasp.DiSCaMB: a software library for aspherical atom model X-ray scattering factor calculations with CPUs and GPUs.On the Charge Density Refinement of Odd-Order Multipoles Invariant under Crystal Point Group Symmetry
P2860
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P2860
Charge-density analysis of an iron-sulfur protein at an ultra-high resolution of 0.48 Å.
description
2016 nî lūn-bûn
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2016年の論文
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2016年学术文章
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2016年学术文章
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2016年学术文章
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2016年学术文章
@zh-my
2016年学术文章
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2016年學術文章
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2016年學術文章
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2016年學術文章
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name
Charge-density analysis of an iron-sulfur protein at an ultra-high resolution of 0.48 Å.
@en
Charge-density analysis of an iron-sulfur protein at an ultra-high resolution of 0.48 Å.
@nl
type
label
Charge-density analysis of an iron-sulfur protein at an ultra-high resolution of 0.48 Å.
@en
Charge-density analysis of an iron-sulfur protein at an ultra-high resolution of 0.48 Å.
@nl
prefLabel
Charge-density analysis of an iron-sulfur protein at an ultra-high resolution of 0.48 Å.
@en
Charge-density analysis of an iron-sulfur protein at an ultra-high resolution of 0.48 Å.
@nl
P2860
P356
P1433
P1476
Charge-density analysis of an iron-sulfur protein at an ultra-high resolution of 0.48 Å.
@en
P2093
P2860
P2888
P304
P356
10.1038/NATURE18001
P407
P577
2016-05-18T00:00:00Z
P6179
1003491658