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Crystallization and preliminary X‐ray crystallographic analysis of phospholipid transfer protein from maize seedlings
Author(s) -
Shin Dong Hae,
Hwang Kwang Yeon,
Kim Kyeong Kyu,
Kim Sangsoo,
Sweet Robert M.,
Suh Se Won
Publication year - 1994
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340190111
Subject(s) - crystallization , crystallography , phospholipid , protein crystallization , x ray , materials science , chemistry , biochemistry , physics , optics , membrane , organic chemistry
Phospholipid transfer protein from maize seedlings has been crystallized using trisodium citrate as precipitant. The crystal belongs to the orthorhombic space group P 2 1 2 1 2 1 with unit cell dimensions of a = 24.46 Å, b = 49.97 Å, and c = 69.99 Å. The presence of one molecule in the asymmetric unit gives a crystal volume per protein mass ( V m ) of 2.36 Å 3 /Da and a solvent content of 48% by volume. The X‐ray diffraction pattern extends at least to 1.6 Å Bragg spacing when exposed to both Cu K α and synchrotron X‐rays. A set of X‐ray data to approximately 1.9 Å Bragg spacing has been collected from a native crystal. © 1994 Wiley‐Liss, Inc.