Structural highlights
Function
[DPOL_BPPH2] This polymerase possesses two enzymatic activities: DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'- to 5'-direction.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
In 1954, Howells and colleagues described an unusual diffraction pattern from imidazole methemoglobin crystals caused by lattice-translocation defects. In these crystals, two identical lattices coexist as a single coherent mosaic block, but are translated by a fixed vector with respect to each other. The observed structure is a weighted sum of the two identical but translated structures, one from each lattice; the observed structure factors are a weighted vector sum of the two structure factors with identical unit amplitudes but shifted phases. A general procedure is described to obtain the unit amplitudes of observed structure factors from a realigned single lattice through an X-ray intensity correction. An application of this procedure is made to determine the crystal structure of phi29 DNA polymerase at 2.2 A resolution using multiple isomorphous replacement and multiwavelength anomalous dispersion methods.
Correction of X-ray intensities from single crystals containing lattice-translocation defects.,Wang J, Kamtekar S, Berman AJ, Steitz TA Acta Crystallogr D Biol Crystallogr. 2005 Jan;61(Pt 1):67-74. Epub 2004, Dec 17. PMID:15608377[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Wang J, Kamtekar S, Berman AJ, Steitz TA. Correction of X-ray intensities from single crystals containing lattice-translocation defects. Acta Crystallogr D Biol Crystallogr. 2005 Jan;61(Pt 1):67-74. Epub 2004, Dec 17. PMID:15608377 doi:10.1107/S0907444904026721
