X-ray crystallography has altered the course of molecular biology. It is largely because of this method that we are able to visualize the structure of molecules in atomic detail. It's important to note that if one knew, in accurate detail, the structure of the active site, or other important regions of an enzyme, then one can fabricate molecules that would bind to those sites and interfere with the enzyme's activity. The present study is on a bacterium known as Thermatoga maritima. The function of this protein is unknown, to date. However, it is known that T. maritima metabolizes many simple and complex carbohydrates. The protein was crystallized, x-ray diffraction was performed, a pattern was obtained, the data was analyzed in order for an electron density map to be calculated and then a model was determined. Since it is a hypothetical protein, there isn't much that is known yet. The fact that T. maritima is related to other organisms mean that if every protein in this organism is to be solved, a library of sequences with corresponding structures can be obtained.
PDF
download
878987797
028-85220240
