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Scientific article
English

Crystallization and preliminary X-ray analysis of the 9 kDa protein of the mouse signal recognition particle and the selenomethionyl-SRP9

Published inFEBS letters, vol. 384, no. 3, p. 219-221
Publication date1996-04-22
Abstract

Two different crystal forms of the 9 kDa protein of the signal recognition particle (SRP9) have been prepared by the hanging drop vapor diffusion technique using 28% (w/v) PEG8000 or 28% saturated ammonium sulphate as precipitant. The crystals are hexagonal bipyramids with average dimensions of 0.2 X 0.1 X 0.1 mm(3) and they diffract to a resolution of 2.3 Angstroms. They belong to the space groups P6(2)22/P6(4)22 or P3(1)21/P3(2)21 with cell dimensions a = b = 63.0 Angstroms, and c = 111.5 Angstroms. Crystals have also been grown from the selenomethionyl protein and multiwavelength data sets have been collected.

eng
Keywords
  • Animals
  • Crystallization
  • Crystallography, X-Ray / instrumentation
  • Crystallography, X-Ray / methods
  • Diffusion
  • Mice
  • Selenomethionine / chemistry
  • Signal Recognition Particle / chemistry
Citation (ISO format)
DOUBLIÉ, Sylvie et al. Crystallization and preliminary X-ray analysis of the 9 kDa protein of the mouse signal recognition particle and the selenomethionyl-SRP9. In: FEBS letters, 1996, vol. 384, n° 3, p. 219–221. doi: 10.1016/0014-5793(96)00316-x
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ISSN of the journal0014-5793
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