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
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