PMID:12454470

Citation	Lemke, CT, Smith, GD and Howell, PL (2002) S-SAD, Se-SAD and S/Se-SIRAS using Cu Kalpha radiation: why wait for synchrotron time? Acta Crystallogr. D Biol. Crystallogr. 58:2096-101
Abstract	The structure of Escherichia coli argininosuccinate synthetase (EAS) has been determined using S-SAD, Se-SAD and S/Se-SIRAS data measured with Cu Kalpha radiation. EAS contains 16 methionines and three cysteines in 455 amino acids. At a wavelength of 1.54 A (Cu Kalpha), the native (S-Met) and derivative (Se-Met) proteins yield anomalous signals of approximately 0.86 and 1.6%, respectively. Highly redundant data were measured to 2.0 A from native and derivative EAS crystals. All three structure determinations were carried out in a highly automated manner using SnB and SOLVE/RESOLVE. Despite the minute Bijvoet differences at 1.54 A, the signal was sufficient to determine the heavy-atom substructure and produce high-quality electron-density maps in all three cases. These maps were readily interpretable by the RESOLVE automated building algorithm, which modeled greater than 75% of all three structures. The success of these methods has profound implications for crystallographers experiencing difficulty with heavy-atom incorporation or with limited access to a synchrotron source.
Links	PubMed
Keywords	Argininosuccinate Synthase/chemistry; Argininosuccinate Synthase/isolation & purification; Escherichia coli/enzymology; Protein Conformation; Synchrotrons
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