Structure resolution easily

Aug 6th, 2022
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How to structure resolution

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in a holiday Junction two homologous duplexes are linked by the reciprocal exchange of a pair of DNA strands the formation of a holiday Junction is initiated by the formation of a d-loop between homologous duplexes in which a strand from one duplex shown here in Gray invades the other duplex shown in pink regions of heteroduplex DNA are formed in which complementary strands from the two different duplexes are paired cleavage of the d-loop and subsequent ligation results in a holiday Junction which links the two duplexes holiday Junctions adopt a planar unfolded structure when they interact with recombination proteins notice that both of the linked duplexes contain regions of homo duplex where graystrand pairs with gray Strand and pink strand pairs with pink Strand and heteroduplex where great strand pairs with pink strand also notice that the holiday Junction involves four DNA strands there are two axes of symmetry in the holiday Junction one horizontal and one vertical strands of the

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In protein X-ray crystallography, resolution is often used as a good indicator of structural quality. Diffraction resolution of protein crystals correlates well with the number of X-ray observables that are used in structure generation and, therefore, with protein coordinate errors.
Resolution is a measure of the quality of the data that has been collected on the crystal containing the protein or nucleic acid.
Most protein structures solved today have a resolution of 1.5 to 2.5 , which means the hydrogen atoms are not visible and there is some uncertainty in the precise location of the heavy atoms.
Resolution is a measure of the quality of the data that has been collected on the crystal containing the protein or nucleic acid.
What is normally referred to as resolution is the nominal resolution ( d h i g h ). This is defined by the smallest distance (typically measured in ) between crystal lattice planes that is resolved in the diffraction pattern, i.e., if this number is lower, the resolution is higher and vice versa.
Abstract. Resolution measures in molecular electron microscopy provide means to evaluate quality of macromolecular structures computed from sets of their two-dimensional (2D) line projections.
The term atomic resolution was defined a long time ago and it is generally accepted to correspond to an electron-density map (or a map calculated using another type of data, for example nuclear density) in which individual atoms can be distinguished.
Resolution is a measure of the quality of the data that has been collected on the crystal containing the protein or nucleic acid.
Most protein structures solved today have a resolution of 1.5 to 2.5 , which means the hydrogen atoms are not visible and there is some uncertainty in the precise location of the heavy atoms.
The resolution for a given crystal (a specific crystal lattice and type of symmetry) is roughly determined by the number of diffraction spots (intensities) collected during a crystallography experiment.

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