Point mutations are frequently used to explore the structure and/or fu
nction of proteins. The ability to predict the structural effects of p
oint mutations would make the planning of such experiments more reliab
le. We have now derived a set of detailed predictive rules based on th
e comparison of crystal structures of point mutants and wild types in
83 cases. Despite the surprising simplicity of these rules, they descr
ibe well the conformational changes in 85% of all point mutant structu
res available at present.