CRYSTALLIZATION OF THE B800-820 LIGHT-HARVESTING COMPLEX FROM RHODOPSEUDOMONAS-ACIDOPHILA STRAIN 7750

被引：14

作者：

GUTHRIE, N

MACDERMOTT, G

COGDELL, RJ

FREER, AA

ISAACS, NW

HAWTHORNTHWAITE, AM

HALLOREN, E

LINDSAY, JG

机构：

[1] UNIV GLASGOW,DEPT BOT,GLASGOW G12 8QQ,SCOTLAND

[2] UNIV GLASGOW,DEPT BIOCHEM,GLASGOW G12 8QQ,SCOTLAND

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1992年 / 224卷 / 02期

关键词：

CRYSTALS; MEMBRANES; PROTEIN; LIGHT-HARVESTING; CRYSTALLOGRAPHY;

D O I：

10.1016/0022-2836(92)91016-I

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 B800-820 light-harvesting complex, an integral membrane protein, from Rhodopseudomonas acidophila strain 7750 has been crystallized. The tabular plates have a hexagonal unit cell of a = b = 121·8 A ̊ and c = 283·1 A ̊ and belong to the space group R32. X-ray diffraction data have been collected to 6 Å resolution, using an area detector on a rotating anode source. The B800-820 light-harvesting complex is comprised of four low molecular weight apoproteins (B800-820α1, B800-820α2, B800-820β1 and B800-820β2). Polyacrylamide gel electrophoresis shows that the complex exists as an oligomeric assembly, with an apparent molecular weight of 92,000. © 1992.

引用

页码：527 / 528

页数：2

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