The crystal structure of pea lectin at 3.0-A resolution

The structure of pea lectin has been determined to 3.0-A resolution based on multiple isomorphous replacement phasing to 6.0-A resolution and a combination of single isomorphous replacement, anomalous scattering, and density modification to 3.0-A resolution. The pea lectin model has been optimized b...

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Veröffentlicht in:	The Journal of biological chemistry 1986-12, Vol.261 (35), p.16518-16527
Hauptverfasser:	Einspahr, H, Parks, E H, Suguna, K, Subramanian, E, Suddath, F L
Format:	Artikel
Sprache:	eng
Schlagworte:	Biological and medical sciences Concanavalin A Crystalline structure Fundamental and applied biological sciences. Psychology Lectins Models, Molecular Molecular biophysics pisum sativum Plant Lectins Protein Conformation proteinas proteine proteins Structure in molecular biology Structure-Activity Relationship X-Ray Diffraction
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