1k6d

Publication Abstract from PubMed

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.

Autotracing of Escherichia coli acetate CoA-transferase alpha-subunit structure using 3.4 A MAD and 1.9 A native data.,Korolev S, Koroleva O, Petterson K, Gu M, Collart F, Dementieva I, Joachimiak A Acta Crystallogr D Biol Crystallogr. 2002 Dec;58(Pt 12):2116-21. Epub 2002, Nov 23. PMID:12454473^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.