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PMID: 15299426 Published · ppublish English Journal Article

Acid pH crystallization of the basic protein lysin from the spermatozoa of red abalone (Haliotis rufescens).

Acta crystallographica. Section D, Biological crystallography ·Vol. 50 ·No. Pt 4 ·1994-07-01 ·Pages 620-6

Diller TC, Shaw A, Stura EA, Vacquier VD, Stout CD

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.

Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Diller T C
The Scripps Research Institute, Department of Molecular Biology, La Jolla, CA 92037-1093, USA.
Shaw A
Stura E A
Vacquier V D
Stout C D
Article Info
Journal
Acta crystallographica. Section D, Biological crystallography
Abbr.
Acta Crystallogr D Biol Crystallogr
ISSN
0907-4449
Published
1994-07-01
Pages
620-6
Language
English
Region
United States
NLM ID
9305878
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