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

• Authors: J. Helliwell , H. Price , A. Deacon , J. Raftery , J. Habash
• Languages of publication: EN

Abstracts

EN

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.

Keywords

EN

87.64.-t; 87.15.-v; 61.12.-q

Discipline

• 87.64.-t: Spectroscopic and microscopic techniques in biophysics and medical physics
• 87.15.-v: Biomolecules: structure and physical properties(for NMR of biomolecules, see 82.56.Pp)

• Publisher: Institute of Physics, Polish Academy of Sciences
• Journal: Acta Physica Polonica A
• Year: 2002
• Volume: 101
• Issue: 5
• Pages: 583-588

Dates

published

2002-05

received

2001-08-31

Contributors

author

J. Helliwell

• Department of Chemistry, University of Manchester, M13 9PL, Manchester, UK

author

H. Price

• Department of Chemistry, University of Manchester, M13 9PL, Manchester, UK

author

A. Deacon

• Department of Chemistry, University of Manchester, M13 9PL, Manchester, UK

author

J. Raftery

• Department of Chemistry, University of Manchester, M13 9PL, Manchester, UK

author

J. Habash

• Department of Chemistry, University of Manchester, M13 9PL, Manchester, UK

References

• 1. D. Vitkup, D. Ringe, G.A. Petsko, M. Karplus, Nat. Struct. Biol., 7, 34, 2000
• 2. A. Deacon, T. Gleichmann, A.J. Kalb (Gilboa), H. Price, J. Raftery, G. Bradbrook, J. Yariv, J.R. Helliwell, Faraday Trans., 93, 4305, 1997
• 3. J. Habash, J. Raftery, S. Weisgerber, A. Cassetta, M. Lehmann, P. Hoghoj, C. Wilkinson, J.W. Campbell, J.R. Helliwell, Faraday Trans., 93, 4313, 1997
• 4. J. Habash, J. Raftery, R. Nuttall, H.J. Price, C. Wilkinson, A.J. Kalb (Gilboa), J.R. Helliwell, Acta Crystallogr. D, 56, 541, 2000
• 5. H.J. Price, Ph.D. thesis, University of Manchester, 1999
• 6. E.H. Snell, N.E. Chayen, J.R. Helliwell, Biochemist, 21, 19, 1999
• 7. A.J. Kalb (Gilboa), D. Myles, J. Habash, J. Raftery, J.R. Helliwell, J. Appl. Crystallogr., 34, 454, 2001
• 8. J.R. Helliwell, C.C. Wilson, in preparation
• 9. Report of the ESS Biology and Biotechnology Science Definition Group, 2001, Engelberg Workshop (copies available from [e-mail])

Identifiers

DOI

10.12693/APhysPolA.101.583