Crystallization and preliminary X-ray crystallographic analysis of phospholipid transfer protein from maize seedlings.
Phospholipid transfer protein from maize seedlings has been crystallized using trisodium citrate as precipitant. The crystal belongs to the orthorhombic space group P2(1)2(1)2(1) with unit cell dimensions of a = 24.46 A, b = 49.97 A, and c = 69.99 A. The presence of one molecule in the asymmetric unit gives a crystal volume per protein mass (Vm) of 2.36 A3/Da and a solvent content of 48% by volume. The X-ray diffraction pattern extends at least to 1.6 A Bragg spacing when exposed to both CuK alpha and synchrotoron X-rays. A set of X-ray data to approximately 1.9 A Bragg spacing has been collected from a native crystal.
Shin
D H
DH
Department of Chemistry, College of Natural Sciences, Seoul National University, Korea.
Hwang
K Y
KY
Kim
K K
KK
Kim
S
S
Sweet
R M
RM
Suh
S W
SW
D000595:Amino Acid Sequence; D002352:Carrier Proteins / Q000737:chemistry* / Q000302:isolation & purification; D003460:Crystallization; D018360:Crystallography, X-Ray; D008565:Membrane Proteins / Q000737:chemistry* / Q000302:isolation & purification; D008969:Molecular Sequence Data; D049294:Phospholipid Transfer Proteins; D010940:Plant Proteins / Q000737:chemistry* / Q000302:isolation & purification; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D013045:Species Specificity; D003313:Zea mays / Q000737:chemistry*
D002352:Carrier Proteins; D008565:Membrane Proteins; D049294:Phospholipid Transfer Proteins; D010940:Plant Proteins