Using surface-bound rubidium ions for protein phasing

S. Korolev; I. Dementieva; R. Sanishvili; W. Minor; Z. Otwinowski; A. Joachimiak

doi:10.1107/S0907444901007302

Using surface-bound rubidium ions for protein phasing

S. Korolev, I. Dementieva, R. Sanishvili, W. Minor, Z. Otwinowski, A. Joachimiak

Research output: Contribution to journal › Article › peer-review

19 Scopus citations

Abstract

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.

Original language	English (US)
Pages (from-to)	1008-1012
Number of pages	5
Journal	Acta Crystallographica Section D: Biological Crystallography
Volume	57
Issue number	7
DOIs	https://doi.org/10.1107/S0907444901007302
State	Published - 2001

ASJC Scopus subject areas

Structural Biology

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abstract = "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.",

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T1 - Using surface-bound rubidium ions for protein phasing

AU - Korolev, S.

AU - Dementieva, I.

AU - Sanishvili, R.

AU - Minor, W.

AU - Otwinowski, Z.

AU - Joachimiak, A.

PY - 2001

Y1 - 2001

N2 - 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.

AB - 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.

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Using surface-bound rubidium ions for protein phasing

Abstract

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