Crystallographic refinement of ricin to 2.5 angstrom

Crystallographic refinement of ricin to 2.5 angstrom

The plant cytotoxin ricin consists of two disulfide-linked chains, each of about 30,000 daltons. An initial model based on a 2.8 angstrom MIR electron density map has been refined against 2.5 angstrom data using rounds of hand rebuilding coupled with either a restrained least squares algorithm or mo...

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Veröffentlicht in:Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 1991-01, Vol.10 (3), p.240-250
Hauptverfasser: Rutenber, E, Katzin, B J, Ernst, S, Collins, E J, Mlsna, D, Ready, M P, Robertus, J D
Format: Artikel
Sprache:eng
Schlagworte:
ricin
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Zusammenfassung:The plant cytotoxin ricin consists of two disulfide-linked chains, each of about 30,000 daltons. An initial model based on a 2.8 angstrom MIR electron density map has been refined against 2.5 angstrom data using rounds of hand rebuilding coupled with either a restrained least squares algorithm or molecular dynamics (XPLOR).
ISSN:0887-3585