Purification, crystallization and preliminary X-ray analysis of the catalytic domain of the Escherichia coli tRNase colicin D.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 62(Pt 1): 29-31, 2006 Jan 01.
Article
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| MEDLINE
| ID: mdl-16511255
ABSTRACT
The tRNase domain of colicin D, which cleaves only tRNA(Arg)s at the 3' side of their anticodon loops, has been expressed in Escherichia coli with its inhibitor protein and purified to a form free from the inhibitor using a low-pH buffer. Crystals were obtained by the hanging-drop vapour-diffusion method at 278 K from a buffer containing 100 mM Tris-HCl pH 8.5, 22% PEG MME 2000 and 1 mM nickel(II) chloride. Diffraction data to 1.05 A resolution were collected at BL41XU, SPring-8. The crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 34.7, b = 65.5, c = 96.5 A.
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1
Banco de datos:
MEDLINE
Asunto principal:
Dominio Catalítico
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Proteínas de Escherichia coli
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Endorribonucleasas
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Escherichia coli
Idioma:
En
Revista:
Acta Crystallogr Sect F Struct Biol Cryst Commun
Año:
2006
Tipo del documento:
Article
País de afiliación:
Japón