Rotation function studies of human C-reactive protein

D. A.A. Myles; S. A. Rule; L. J. DeLucas; Y. S. Babu; Y. Xu; J. E. Volanakis; C. E. Bugg; S. Bailey; T. J. Greenhough

doi:10.1016/0022-2836(90)90373-T

Rotation function studies of human C-reactive protein

D. A.A. Myles, S. A. Rule, L. J. DeLucas, Y. S. Babu, Y. Xu, J. E. Volanakis, C. E. Bugg, S. Bailey, T. J. Greenhough

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18 Scopus citations

Abstract

Rotation function studies of two tetragonal crystal forms of human C-reactive protein have confirmed the pentameric structure of the molecule. The two crystal forms have space groups P4₁22 (I) and P4₂22 (II) with closely similar unit cells and are often twinned together. Investigation of the crystallization conditions indicates that dissociation heterogeneity has been a major limiting factor in the reproducible growth of good single crystals. The orientation of the pentameric molecule is shown to be almost identical in both forms, about the axial direction ω = 57 °, φ = 45 °, i.e. 57 ° away from c in the (110) plane.

Original language	English
Pages (from-to)	491-496
Number of pages	6
Journal	Journal of Molecular Biology
Volume	216
Issue number	3
DOIs	https://doi.org/10.1016/0022-2836(90)90373-T
State	Published - Dec 5 1990
Externally published	Yes

Funding

We gratefully acknowledge financial support from the MRC and SERC to (T.J.G.) and thank Dr A. C. Bloomer for comments and discussion.

Funders	Funder number
Connecticut State Emergency Response Commission
Medical Research Council

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title = "Rotation function studies of human C-reactive protein",

abstract = "Rotation function studies of two tetragonal crystal forms of human C-reactive protein have confirmed the pentameric structure of the molecule. The two crystal forms have space groups P4122 (I) and P4222 (II) with closely similar unit cells and are often twinned together. Investigation of the crystallization conditions indicates that dissociation heterogeneity has been a major limiting factor in the reproducible growth of good single crystals. The orientation of the pentameric molecule is shown to be almost identical in both forms, about the axial direction ω = 57 °, φ = 45 °, i.e. 57 ° away from c in the (110) plane.",

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T1 - Rotation function studies of human C-reactive protein

AU - Myles, D. A.A.

AU - Rule, S. A.

AU - DeLucas, L. J.

AU - Babu, Y. S.

AU - Xu, Y.

AU - Volanakis, J. E.

AU - Bugg, C. E.

AU - Bailey, S.

AU - Greenhough, T. J.

PY - 1990/12/5

Y1 - 1990/12/5

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AB - Rotation function studies of two tetragonal crystal forms of human C-reactive protein have confirmed the pentameric structure of the molecule. The two crystal forms have space groups P4122 (I) and P4222 (II) with closely similar unit cells and are often twinned together. Investigation of the crystallization conditions indicates that dissociation heterogeneity has been a major limiting factor in the reproducible growth of good single crystals. The orientation of the pentameric molecule is shown to be almost identical in both forms, about the axial direction ω = 57 °, φ = 45 °, i.e. 57 ° away from c in the (110) plane.

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Rotation function studies of human C-reactive protein

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