title: Using surface-bound rubidium ions for protein phasing.
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.
authors: Biosciences Division and Structural Biology Center, Argonne National Laboratory, 9700 South Cass Avenue, Building 202, Argonne, IL 60439, USA.
authors: S
authors: S
authors: Korolev
authors: I
authors: I
authors: Dementieva
authors: R
authors: R
authors: Sanishvili
authors: W
authors: W
authors: Minor
authors: Z
authors: Z
authors: Otwinowski
authors: A
authors: A
authors: Joachimiak
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry*; D018834:Chaperonin 60 / Q000737:chemistry; D008958:Models, Molecular; D012413:Rubidium / Q000737:chemistry*; D013499:Surface Properties; D016963:Thermus thermophilus / Q000737:chemistry
chemical_list: D001426:Bacterial Proteins; D018834:Chaperonin 60; D012413:Rubidium