Using surface-bound rubidium ions for protein phasing

Rubidium is a monovalent metal that can be used as a counterion in protein solutions. X‐ray anomalous scattering from rubidium ions bound to the protein surface was used for phasing of the crystal structure of the hsp60 apical domain from Thermus thermophilus. Multiple‐wavelength anomalous dispersio...

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Bibliographic Details
Published in:Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2001-07, Vol.57 (7), p.1008-1012
Main Authors: Korolev, S., Dementieva, I., Sanishvili, R., Minor, W., Otwinowski, Z., Joachimiak, A.
Format: Article
Language:English
Subjects:
anomalous diffraction
Bacterial Proteins - chemistry
Chaperonin 60 - chemistry
hsp60 apical domain
Models, Molecular
Rubidium - chemistry
rubidium ions
Surface Properties
Thermus thermophilus - chemistry
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Summary:Rubidium is a monovalent metal that can be used as a counterion in protein solutions. X‐ray anomalous scattering from rubidium ions bound to the protein surface was used for phasing of the crystal structure of the hsp60 apical domain from Thermus thermophilus. Multiple‐wavelength anomalous dispersion (MAD) data were collected from a crystal obtained from a solution containing 0.2 M rubidium salt. One molecule of protein (147 amino acids) binds one well ordered and one poorly ordered Rb atom. Phases calculated with the program SHARP were sufficient for automatic tracing and side‐chain assignment using the program ARP/wARP. The data show that bound rubidium ions can be used to determine protein structures and to study the interaction of monovalent metal ions with proteins and other macromolecules.
ISSN:1399-0047
0907-4449
1399-0047
DOI:10.1107/S0907444901007302