title: Autotracing of Escherichia coli acetate CoA-transferase alpha-subunit structure using 3.4 A MAD and 1.9 A native data.
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.
authors.affiliation: Biosciences Division and Structural Biology Center, Argonne National Laboratory, 9700 South Cass Avenue, Argonne, IL 60439, USA.
authors.forename: S
authors.initials: S
authors.lastname: Korolev
authors.forename: O
authors.initials: O
authors.lastname: Koroleva
authors.forename: K
authors.initials: K
authors.lastname: Petterson
authors.forename: M
authors.initials: M
authors.lastname: Gu
authors.forename: F
authors.initials: F
authors.lastname: Collart
authors.forename: I
authors.initials: I
authors.lastname: Dementieva
authors.forename: A
authors.initials: A
authors.lastname: Joachimiak
mesh_terms: D015256:Coenzyme A-Transferases / Q000737:chemistry*; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000201:enzymology*; D029968:Escherichia coli Proteins / Q000737:chemistry*; D008958:Models, Molecular; D011487:Protein Conformation
chemical_list: D029968:Escherichia coli Proteins; D015256:Coenzyme A-Transferases