TECHNOLOGY FOCUS - BIOTECHNOLOGY - Preferred Method: Preserving the cell extract comprises: dissolving the first non-reducing sugar alcohol in the cell extract to provide a cell extract solution; manipulating the cell extract solution to prevent fouling; and drying the cell extract solution. Manipulating the cell extract solution comprises at least one of filtering the cell extract solution or adding an anti-fouling agent to the cell extract solution. Preserving the reaction buffer comprises: dissolving the second non-reducing sugar alcohol in the reaction buffer to provide a reaction buffer solution; manipulating the reaction buffer solution to prevent fouling; and drying the reaction buffer solution. Manipulating the reaction buffer solution comprises at least one of filtering the reaction buffer solution or adding an anti-fouling agent to the reaction buffer solution. Preserving the energy source comprises storing the energy source in a dry form. The method further comprises reconstituting the cell-free protein expression system via: adding water to the preserved cell extract; adding water to the preserved reaction buffer; and combining the preserved cell extract, the preserved reaction buffer, the energy source, and an expression construct to provide a reconstituted cell-free protein expression system. The reconstituted cell-free protein expression system performs transcription and translation. Preferred Components: The anti- fouling agent comprises an RNAse inhibitor and/or an antibiotic that does not interfere with transcription or translation. The cell extract comprises: a bacterial extract, a yeast extract, a fungal extract, an archaeal extract, a plant cell extract, a mammalian cell extract, an insect cell extract and/or combination of purified proteins for reconstituting protein expression; or an Escherichia coli extract, a Saccharomyces cerevisae extract, a wheat germ extract, a reticulocyte extract, a HeLa cell extract, a Spodoptera frugiperda extract and/or Trichoplusia ni extract. The expression enhancing agents comprise folinic acid, cyclic adenosine monophosphate, transfer RNA, nicotinamide adenine dinucleotide, coenzyme A, oxalic acid, succinic acid, 2-oxoglutaric acid, malic acid and/or a reducing agent.    TECHNOLOGY FOCUS - ORGANIC CHEMISTRY - Preferred Components: The first non-reducing sugar alcohol and the second non-reducing sugar alcohol comprises trehalose. The reaction buffer comprises nucleotides, amino acids, stabilizing agents, expression enhancing agents, salts and/or enzymes. The stabilizing agents comprise 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid, bis (2 -hydroxyethyl)amino -tris (hydroxymethyl)methane, polyethylene glycol, spermidine, putrescine, chaperones and/or detergents. The salts comprise potassium glutamate and/or ammonium acetate. The enzymes comprise creatine kinase. The energy source comprises creatine phosphate, phosphoenol pyruvate, pyruvate, glutamate, acetyl phosphate, glucose, glucose-6-phos- phate, maltodextrin, acetate phosphate, 3-phosphoglycerate and/or fructose-1,6-bisphosphate. EXAMPLE - The cell extract was dried. 0.6 M Trehalose was added to E. coli extract, and the resulting solution was filtered using a 0.2 mu m spin filter. 25 mu l drops of, of the filtered solution were dispensed onto a silicon sheet and were dried in a 37 degrees C incubator. Then reaction buffer components were preserved. Default reaction buffer without magnesium acetate or creatine phosphate was prepared, and 0.6 M trehalose was added. The resulting solution was filtered using a 0.2 mu m spin filter. Then, 29.35 mu l drops of the filtered solutions were dispensed onto a silicon sheet and were dried in a 37 degrees C incubator. Finally obtained cell-free protein expression system components of creatine phosphate in dry form were stored at 37 degrees C.