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Updated: Aug 23, 2026

Protein Crystallization for X-ray Crystallography
Published on: January 16, 2011
Acid pH crystallization of the basic protein lysin from the spermatozoa of red abalone (Haliotis rufescens)
T C Diller1, A Shaw, E A Stura
1The Scripps Research Institute, Department of Molecular Biology, La Jolla, CA 92037-1093, USA.
Abstract:
A new crystal form of dimeric red lysin, a distinctly basic protein (M(r) = 16 070) from the red abalone (Haliotis rufescens), has been obtained using ammonium sulfate as precipitant with a sodium citrate-boric acid-citric acid buffer at pH 4.5. The acid pH crystal form resulted from a study aimed at developing conditions favorable to the sitting-drop vapor-diffusion crystallization of other abalone lysins which do not crystallize at neutral or basic pH conditions. The space group is P222(1) with cell dimensions a = 51.2, b = 47.0, c = 123.8 A and two molecules per asymmetric unit.

