Open AccessAutotracing of Escherichia coli acetate CoA‐transferase α‐subunit structure using 3.4 Å MAD and 1.9 Å native data
Author(s) -
Korolev S.,
Koroleva O.,
Petterson K.,
Gu M.,
Collart F.,
Dementieva I.,
Joachimiak A.
Publication year - 2002
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
ISSN - 1399-0047
DOI - 10.1107/s0907444902017055
Subject(s) - structural genomics , protein subunit , resolution (logic) , transferase , escherichia coli , chemistry , structural biology , crystallography , crystal structure , protein structure , chromatography , biochemistry , enzyme , computer science , gene , artificial intelligence
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 Å) from crystals of SeMet‐labeled protein can be successfully used for automated structure determination. The crystal structure of acetate CoA‐transferase α‐subunit was solved using 3.4 Å multiwavelength anomalous dispersion data collected from a crystal containing SeMet‐substituted protein and 1.9 Å data collected from a native protein crystal.