Protein arrays continue to increase in importance as tools for analysis of biological samples. This paper describes a new method for preparing bioarrays that is compatible with high throughput manufacturing. First, a native oxide terminated silicon substrate is coated with a monolayer of a polyethylene-glycol-containing silane. The coated substrate is then placed beneath a microlens array (MA) and the array is irradiated with a brief (4 ns) pulse of 532 nm laser light. The MA focuses the laser light onto the substrate, causing monolayer removal. The microlenses in the array employed in this work are square packed and have a spacing of 100 mu m, that is, there are 10000 microlenses/cm(2) in the optic and therefore 10000 spots/cm(2) on surfaces patterned with this array. The patterned substrate is then immersed in a dilute (10(-5) M) solution of a protein. Time-of-flight secondary ion mass spectrometry shows that all of the proteins studied, including avidin, BSA, ferritin, lysozyme, myoglobin, protein A, and streptavidin, adsorb selectively into the spots in the array. The stability of these adsorbed proteins is shown. The retention of activity of avidin after adsorption is demonstrated. Protein localization on the arrays is demonstrated using a microfluidic spotter. Additionally, it is shown that this method can be used to confirm the location of the metal (iron) in ferritin. It should be possible to generalize this analytical method to other metals that are loaded into ferritin