Literature DB >> 15299426

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

T C Diller1, A Shaw, E A Stura, V D Vacquier, C D Stout.   

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.

Entities:  

Year:  1994        PMID: 15299426     DOI: 10.1107/S0907444993013356

Source DB:  PubMed          Journal:  Acta Crystallogr D Biol Crystallogr        ISSN: 0907-4449


  2 in total

1.  Relative effectiveness of various anions on the solubility of acidic Hypoderma lineatum collagenase at pH 7.2.

Authors:  C Carbonnaux; M Ries-Kautt; A Ducruix
Journal:  Protein Sci       Date:  1995-10       Impact factor: 6.725

2.  Crystal structure and subunit dynamics of the abalone sperm lysin dimer: egg envelopes dissociate dimers, the monomer is the active species.

Authors:  A Shaw; P A Fortes; C D Stout; V D Vacquier
Journal:  J Cell Biol       Date:  1995-09       Impact factor: 10.539

  2 in total

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