The detection of sub-units within the crystallographic asymmetric unit

Rossmann, Michael G.; Blow, D. M.

doi:10.1107/s0365110x62000067

Cited by 897 publications

(418 citation statements)

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“…self-rotation search (Rossmann & Blow, 1962) gave an inCrystals of human MnSOD were grown in 2-methyldication for a noncrystallographic twofold axis about 11' 2,4-pentanediol (MPD) from preparations in which the from the y-axis. The results, however, were not conclumetal content before crystallization was typically 0.65-sive (the peak height was about 53% of the origin peak; 0.85 Mn atoms per subunit (M.M.…”

Section: Data Collectionmentioning

confidence: 99%

Comparison of the crystal structures of genetically engineered human manganese superoxide dismutase and manganese superoxide dismutase from thermus thermophilus: Differences in dimer–dimer interaction

et al. 1993

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The three‐dimensional X‐ray structure of a recombinant human mitochondrial manganese superoxide dismutase (MnSOD) (chain length 198 residues) was determined by the method of molecular replacement using the related structure of MnSOD from Thermus thermophilus as a search model. This tetrameric human MnSOD crystallizes in space group P21212 with a dimer in the asymmetric unit (Wagner, U.G., Werber, M.M., Beck, Y., Hartman, J.R., Frolow, F., & Sussman, J.L., 1989, J. Mol. Biol. 206, 787–788). Refinement of the protein structure (3, 148 atoms with Mn and no solvents), with restraints maintaining noncrystallographic symmetry, converged at an R‐factor of 0.207 using all data from 8.0 to 3.2 Å resolution and group thermal parameters. The monomer–monomer interactions typical of bacterial Fe‐ and Mn‐containing SODs are retained in the human enzyme, but the dimer–dimer interactions that form the tetramer are very different from those found in the structure of MnSOD from T. thermophilus. In human MnSOD one of the dimers is rotated by 84° relative to its equivalent in the thermophile enzyme. As a result the monomers are arranged in an approximately tetrahedral array, the dimer–dimer packing is more intimate than observed in the bacterial MnSOD from T. thermophilus, and the dimers interdigitate. The metal—ligand interactions, determined by refinement and verified by computation of omit maps, are identical to those observed in T. thermophilus MnSOD.

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Section: Data Collectionmentioning

confidence: 99%

Comparison of the crystal structures of genetically engineered human manganese superoxide dismutase and manganese superoxide dismutase from thermus thermophilus: Differences in dimer–dimer interaction

et al. 1993

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“…It is, therefore, akin to the ''common-lines'' procedure of Crowther et al (1970a) and could be compared to a ''self-rotation function'' in crystallography (Rossmann and Blow, 1962). Although these calculations are quite time-consuming, the orientation of any number of projections can be determined simultaneously because the right-hand sides of (10) are dependent only on ( , , ) and not on Q pq .…”

Section: Finding the Orientation Of An Objectmentioning

confidence: 99%

“…., S) be the rotation matrices generated by the sequential symmetry operators such as those given in Table II. Let [␣] and [␤] be deorthogonalization and orthogonalization matrices for the h-cell (see Rossmann and Blow, 1962). Then, (Rossmann and Blow, 1962) and…”

Section: Differentiating Between Crystallographic and Noncrystallogramentioning

confidence: 99%

Cryo-Electron-Microscopy Reconstruction of Partially Symmetric Objects

Rossmann

Tao

1999

Journal of Structural Biology

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“…and O.D.) have independently solved the Tb-parvalbumin structure by the molecular replacement technique [26], using 3.2 A data measured with CuK, radiation and the known carp parvalbumin molecule as a model. The carp parvalbumin structure could thus be superimposed onto our MAD map, and proved to fit nicely the electron density in regions of identical amino acid sequences as shown in fig.1.…”

Section: Resultsmentioning

confidence: 99%

Crystal structure study of Opsanus tau parvalbumin by multiwavelength anomalous diffraction

et al. 1985

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The crystal structure of a small calcium-binding protein, the parvalbumin I& from Opsanus tau in which Tb was substituted for Ca, has been analysed by multiwavelength anomalous diffraction. Data at a resolution of 2.3 A were collected at three wavelengths near the L, absorption edge of Tb (1.645-1.650 A), using the synchrotron radiation emitted by a storage ring and a multiwire proportional counter. The phases of the reflections were determined from this single derivative, without native data. Prior to any refinement, the resulting electron density map shows a good agreement with the model of the homologous carp parvalbumin in regions of identical amino-acid sequence.

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The detection of sub-units within the crystallographic asymmetric unit

Cited by 897 publications

References 1 publication

Comparison of the crystal structures of genetically engineered human manganese superoxide dismutase and manganese superoxide dismutase from thermus thermophilus: Differences in dimer–dimer interaction

Comparison of the crystal structures of genetically engineered human manganese superoxide dismutase and manganese superoxide dismutase from thermus thermophilus: Differences in dimer–dimer interaction

Cryo-Electron-Microscopy Reconstruction of Partially Symmetric Objects

Crystal structure study of Opsanus tau parvalbumin by multiwavelength anomalous diffraction

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