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.
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