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Purification and crystallization of Escherichia coli oligoribonuclease by Tristan J. Fiedler; Helen A. Vincent; Yuhong Zuo; Orit Gavrialov; Arun Malhotra is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is Purification and crystallization of Escherichia coli oligoribonuclease about?

Oligoribonuclease (Orn) is an essential 3 H -to-5 H hydrolytic exoribonuclease which degrades short oligoribonucleotides to 5 H mononucleotides. Escherichia coli Orn has been crystallized under several different conditions using ammonium sulfate, sodium citrate and sodium acetate as precipitants. Both native and selenomethioninelabeled oligoribonuclease (SeMet-Orn) can be crystallized at room temperature in 1.4±1.55 M sodium citrate. The SeMet-Orn crystals diffract to 2.2 A Ê resolution and belong to space group P2 1 2 1 2 1 , with unit-cell parameters a = 70.43, b = 72.87, c = 147.76 A Ê , and two dimers in the asymmetric unit. When grown in the presence of manganese, a second crystal form (Mn-SeMet-Orn) was obtained containing a single dimer per asymmetric unit (P2 1 2 1 2 1 ; a = 63.74, b = 74.31, c = 74.19 A Ê ). Finally, a hexagonal crystal form was obtained using sodium acetate as a precipitant (a = 91.5, b = 91.5, c = 111.1 A Ê ). This crystal (Zn-ApUp-Orn) belongs to the P6 5 space group and has three oligoribonuclease molecules per asymmetric unit.

Who reads Purification and crystallization of Escherichia coli oligoribonuclease?

Author

Tristan J. Fiedler; Helen A. Vincent; Yuhong Zuo; Orit Gavrialov; Arun Malhotra

Publisher

International Union of Crystallography; Blackwell Publishing Inc.; International Union of Crystallography (IUCr) (ISSN 0907-4449)

Published

2004

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)