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Three-dimensional crystals of the light-harvesting chlorophyll a/b protein complex from pea chloroplasts.

Abstract：

:Two forms of three-dimensional crystals of the light-harvesting chlorophyll a/b protein complex from pea have been obtained. Crystals of one form grew as hexagonal plates measuring up to 150 micron across and 2 to 3 micron in thickness. Electron diffraction patterns of thin hexagonal plates showed sharp reflections to a resolution of 3.7 A on a hexagonal reciprocal lattice. The unit cell in projection (a = 127.0 A) and the symmetry of the diffraction pattern (6 mm) suggested that the hexagonal plates were highly ordered stacks of two-dimensional crystals suitable for structure analysis by electron microscopy and image processing. Crystals of a second form grew as dark green octahedra measuring roughly 0.5 mm across. Low-resolution X-ray diffraction patterns suggested a large cubic unit cell (a = 390 A). SDS/polyacrylamide gel electrophoresis of single octahedral crystals showed the same polypeptide composition as the starting solution, one major band at 24,000 apparent molecular weight and two satellite bands of 23,000 and 23,500 apparent molecular weight.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Kühlbrandt W

doi

10.1016/0022-2836(87)90255-5

subject

Has Abstract

pub_date

1987-04-20 00:00:00

pages

757-62

issue

4

eissn

0022-2836

issn

1089-8638

pii

0022-2836(87)90255-5

journal_volume

194

pub_type

杂志文章

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