PMID:12454473
| Citation |
Korolev, S, Koroleva, O, Petterson, K, Gu, M, Collart, F, Dementieva, I and Joachimiak, A (2002) Autotracing of Escherichia coli acetate CoA-transferase alpha-subunit structure using 3.4 A MAD and 1.9 A native data. Acta Crystallogr. D Biol. Crystallogr. 58:2116-21 |
|---|---|
| Abstract |
The automation of protein structure determination is an essential component for high-throughput structural analysis in protein X-ray crystallography and is a key element in structural genomics. This highly challenging undertaking relies at present on the availability of high-quality native and derivatized protein crystals diffracting to high or moderate resolution, respectively. Obtaining such crystals often requires significant effort. The present study demonstrates that phases obtained at low resolution (>3.0 A) from crystals of SeMet-labeled protein can be successfully used for automated structure determination. The crystal structure of acetate CoA-transferase alpha-subunit was solved using 3.4 A multi-wavelength anomalous dispersion data collected from a crystal containing SeMet-substituted protein and 1.9 A data collected from a native protein crystal. |
| Links | |
| Keywords |
Coenzyme A-Transferases/chemistry; Crystallography, X-Ray; Escherichia coli/enzymology; Escherichia coli Proteins/chemistry; Models, Molecular; Protein Conformation |
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