Purification, crystallization and preliminary X-ray diffraction analysis of water-soluble chlorophyll-binding protein from Chenopodium album.
A water-soluble chlorophyll-binding protein (WSCP) with photoconvertibility from Chenopodium album was extracted, purified and crystallized in a darkroom. Green crystals suitable for data collection appeared in about 10 d. A native data set was collected to 2.0 A resolution at 100 K. The space group of the crystal was determined to be orthorhombic I222 or I2(1)2(1)2(1), with unit-cell parameters a = 48.13, b = 60.59, c = 107.21 A. Preliminary analysis of the X-ray data indicated that there is one molecule per asymmetric unit.
Ohtsuki
Takayuki
T
Department of Bimolecular Science, Faculty of Science, Toho University, Miyama 2-2-1, Funabashi, Chiba 274-8510, Japan.
Ohshima
Shigeru
S
Uchida
Akira
A
D027462:Chenopodium / Q000737:chemistry*; D003460:Crystallization; D045342:Light-Harvesting Protein Complexes / Q000737:chemistry* / Q000302:isolation & purification; D010940:Plant Proteins / Q000737:chemistry / Q000302:isolation & purification; D012639:Seeds / Q000737:chemistry*; D014961:X-Ray Diffraction
D045342:Light-Harvesting Protein Complexes; D010940:Plant Proteins