CHARACTERIZATION OF CRYSTALS OF THE THERMOSTABLE DNA-POLYMERASE-I FROM THERMUS-AQUATICUS

Thermus aquaticus DNA polymerase I is an enzyme that is of both physio logical and technological interest. It carries out template-directed p olymerization of DNA at elevated temperatures and is widely used in po lymerase chain reaction (PCR), We have obtained crystals of the enzyme that diffracts X-rays to at least 3.0 Angstrom resolution in a cubic space group, Determination of the three-dimensional structure of the n ative enzyme along with those of relevant complexes will greatly enhan ce our knowledge of molecular events involved in DNA replication, will permit improvements in PCR, and will add to our knowledge of the stru ctural bases of thermostability in proteins. (C) 1995 Wiley-Liss, Inc.