International
Tables for
Crystallography
Volume F
Crystallography of biological macromolecules
Edited by E. Arnold, D. M. Himmel and M. G. Rossmann

International Tables for Crystallography (2012). Vol. F, ch. 22.1, p. 707   | 1 | 2 |

Section 22.1.3.3.2. Solvent-accessible surface (SAS)

M. Gersteina* and F. M. Richardsa

aDepartment of Molecular Biophysics & Biochemistry, 266 Whitney Avenue, Yale University, PO Box 208114, New Haven, CT 06520, USA
Correspondence e-mail:  Mark.Gerstein@yale.edu

22.1.3.3.2. Solvent-accessible surface (SAS)

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The solvent-accessible surface is convex and closed, with defined areas assignable to each individual atom (Lee & Richards, 1971[link]). However, the individual calculated values vary in a complex fashion with variations in the radii of the probe and protein atoms. This radius is frequently, but not always, set at a value considered to represent a water molecule (1.4 Å). The total SAS area increases without bound as the size of the probe increases.

References

Lee, B. & Richards, F. M. (1971). The interpretation of protein structures: estimation of static accessibility. J. Mol. Biol. 55, 379–400.








































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