Solid-state electron transport (ETp) via a monolayer of immobilized azurin (Az) was examined by conducting probe atomic force microscopy (CP-AFM), as a function of both temperature (248-373K) and applied tip force (6-15 nN). At low forces, ETp via holo-Az (with Cu(2+)) is temperature-independent, but thermally activated via the Cu-depleted form of Az, apo-Az. While this observation agrees with those of macroscopic-scale measurements, we find that for holo-Az the mechanism of ETp at high temperatures changes upon an increase in the force applied by the tip to the proteins; namely, above 310 K and forces >6 nN ETp becomes thermally activated. This is in contrast to apo-Az, where increasing applied force causes only small monotonic increases in currents due to decreased electrode separation. The distinct ETp temperature dependence of holo- and apo-Az is assigned to a difference in structural response to pressure between the two protein forms. An important implication of these CP-AFM results (of measurements over a significant temperature range) is that for reliable ETp measurements on flexible macromolecules, such as proteins, the pressure applied during the measurements should be controlled or at least monitored.