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Crystallization and preliminary X-ray analysis of human S100A13.

ABSTRACT: 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).

SUBMITTER: Imai FL

PROVIDER: S-EPMC2225202 | biostudies-literature | 2006 Nov

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray analysis of human S100A13.

Imai Fabiana Lica FL Nagata Koji K Yonezawa Naoto N Yu Jinyan J Ito Eriko E Kanai Saeko S Tanokura Masaru M Nakano Minoru M

Acta crystallographica. Section F, Structural biology and crystallization communications 20061020 Pt 11

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 ...[more]

PMID: 17077500

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