Crystallization and preliminary X-ray analysis of human S100A13.
S100A13 is a member of the S100 family of EF-hand-containing calcium-binding proteins and plays an important role in the secretion of fibroblast growth factor-1 and interleukin 1alpha, two pro-angiogenic factors released by the endoplasmic reticulum/Golgi-independent non-classical secretory pathway. Human S100A13 was heterologously expressed in Escherichia coli, purified and crystallized by the hanging-drop vapour-diffusion method using PEG 3350 as the precipitant. The crystals diffracted X-rays from a synchrotron-radiation source to 1.8 A resolution and the space group was assigned as primitive orthorhombic P2(1)2(1)2(1).
Imai
Fabiana Lica
FL
Department of Chemistry, Faculty of Science, Chiba University, 1-33 Yayoi-cho, Inage-ku, Chiba 263-8522, Japan.
Nagata
Koji
K
Yonezawa
Naoto
N
Yu
Jinyan
J
Ito
Eriko
E
Kanai
Saeko
S
Tanokura
Masaru
M
Nakano
Minoru
M
D000595:Amino Acid Sequence; D003001:Cloning, Molecular; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000235:genetics; D006801:Humans; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification; D009418:S100 Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification
D010446:Peptide Fragments; D011994:Recombinant Proteins; D009418:S100 Proteins; C511523:S100A13 protein, human