ACID PH CRYSTALLIZATION OF THE BASIC-PROTEIN LYSIN FROM THE SPERMATOZOA OF RED ABALONE (HALIOTIS-RUFESCENS)

被引:4
作者
DILLER, TC
SHAW, A
STURA, EA
VACQUIER, VD
STOUT, CD
机构
[1] SCRIPPS RES INST, DEPT MOLEC BIOL, LA JOLLA, CA 92037 USA
[2] UNIV CALIF SAN DIEGO, SCRIPPS INST OCEANOG, CTR MARINE BIOMED & BIOTECHNOL, LA JOLLA, CA 92093 USA
来源
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 1994年 / 50卷
关键词
D O I
10.1107/S0907444993013356
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
A new crystal form of dimeric red lysin, a distinctly basic protein (M(r) = 16070) 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 angstrom and two molecules per asymmetric unit.
引用
收藏
页码:620 / 626
页数:7
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