CRYSTALLIZATION OF THE C-TERMINAL DOMAIN OF RABBIT SERUM HEMOPEXIN

被引：8

作者：

BAKER, HM ^{[1
]}

NORRIS, GE ^{[1
]}

MORGAN, WT ^{[1
]}

SMITH, A ^{[1
]}

BAKER, EN ^{[1
]}

机构：

[1] UNIV MISSOURI,SCH BIOL SCI,KANSAS CITY,MO 64110

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1993年 / 229卷 / 01期

关键词：

HEMOPEXIN; CRYSTALLIZATION; DEGLYCOSYLATION; DOMAINS; HEME-BINDING;

D O I：

10.1006/jmbi.1993.1025

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The C-terminal domain of rabbit serum hemopexin, comprising residues 215 to 435, has been crystallized following removal of the attached carbohydrate using the endoglycosidase Endo F. The crystals, grown by vapour diffusion from solutions containing polyethylene glycol 1500, are orthorhombic, with cell dimensions a = 41.0 AÅ, b = 64.2 AÅ, c = 85.2 AÅ, space group P212121, and one molecule in the asymmetric unit. The crystals diffract to 2.4 AÅ resolution and are suitable for X-ray structure analysis. © 1993 Academic Press, Inc.

引用

页码：251 / 252

页数：2

共 12 条

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