Biochemistry laboratories often use in vitro studies to explore ATP-dependent molecular processes. Enzyme inhibitors of ATP-dependent enzymes such as kinases are needed to examine the binding sites and transition states involved in ATP-dependent reactions. ATP analogs are also used in X-ray crystallography to determine a protein structure in complex with ATP, often together with other substrates. Most useful ATP analogs cannot be hydrolyzed as ATP would be; instead they trap the enzyme in a structure closely related to the ATP-bound state. Adenosine 5′-(γ-thiotriphosphate) is an extremely common ATP analog in which one of the gamma-phosphate oxygens is replaced by a sulfur atom; this anion is hydrolyzed at a dramatically slower rate than ATP itself and functions as an inhibitor of ATP-dependent processes. In crystallographic studies, hydrolysis transition states are modeled by the bound vanadate ion. However, caution is warranted in interpreting the results of experiments using ATP analogs, since some enzymes can hydrolyze them at appreciable rates at high concentration. 
Now this brings us to the next part - how do we go from glucose to ATP? This is achieved through the process of "oxidation" - and this is carried out through a series of metabolic pathways. Complex chemical transformations in the cell occur in a series of separate reactions to form each pathway, and each reaction is catalyzed by a specific enzyme. Interestingly, metabolic pathways are similar in all organisms, from bacteria to humans. In eukaryotes (plants and animals) many of the metabolic pathways are compartmentalized, with certain reactions occurring in specific organelles. Basically, cells trap free energy released from the breakdown (metabolism) of glucose. This energy gets trapped in the ATP as it converts from ADP to ATP by the addition of phosphate.