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Complementarity of Neutron and Ultrahigh Resolution Synchrotron X-Ray Protein Crystallography Studies: Results with Concanavalin A at Cryo and Room Temperature

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Helliwell J., Price H., Deacon A., Raftery J., Habash J.

Acta Physica Polonica A

2002

vol. 101

issue 5

583-588

The complementarity of synchrotron derived ultrahigh resolution X-ray and neutron protein crystallography is explored via an ensemble of plant lectin concanavalin A crystal structures. Thus a resume of a study of a cryo 0.94Å and a neutron (+X-ray) protein crystal 2.4Å structure at room temperature is made and these are then compared in their efficiency to determine the positions of the bound solvent atoms i.e. as hydrogens or deuteriums. First results are also presented of comparisons of two ultrahigh resolution protein crystal structures, the 0.94Å and a new 0.92Å structure. Thus the variability of the two cryo structures, at very fine detail, is described; this variability is in the multiple occupancies of side chains. Overall, one can see that a "complete" structure definition, with today's experimental capabilities, is possible and can include structure ensemble variations.

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1 Acta Physica Polonica A

1 2002

1 Deacon A.

1 Habash J.

1 Helliwell J.

1 Price H.

1 Raftery J.

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Complementarity of Neutron and Ultrahigh Resolution Synchrotron X-Ray Protein Crystallography Studies: Results with Concanavalin A at Cryo and Room Temperature