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Autotracing of E. coli acetate CoA transferase {alpha}-subunit structure using 3.4 {angstrom} MAD and 1.9 {angstrom} native data.

Journal Article · · Acta Crystallogr. D
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 Angstroms multiwavelength anomalous dispersion data collected from a crystal containing SeMet-substituted protein and 1.9 A data collected from a native protein crystal.
Research Organization:
Argonne National Laboratory (ANL)
Sponsoring Organization:
NIH; SC
DOE Contract Number:
AC02-06CH11357
OSTI ID:
949622
Report Number(s):
ANL/BIO/JA-42609
Journal Information:
Acta Crystallogr. D, Journal Name: Acta Crystallogr. D Journal Issue: Pt. 12 ; Dec. 2002 Vol. 58
Country of Publication:
United States
Language:
ENGLISH