Abstract
Human autocrine motility factor (hAMF), a tumor-secreted cytokine which stimulates cell migration in vitro and metastasis in vivo, has been crystallized by the hanging-drop vapour diffusion method. The crystals belong to an orthorhombic space group P212121 with the cell dimensions of a = 80.79 A, b = 107.1 A, and c = 270.9 A. There are two dimers per asymmetric unit. The crystals diffract to at least 2.0 A resolution and are suitable for X-ray structure analysis at high resolution.
Keywords: Crystallization, Motility Factor, cytokine
Protein & Peptide Letters
Title: Crystallization and Preliminary X-Ray Crystallographic Studies of Human Autocrine Motility Factor
Volume: 8 Issue: 4
Author(s): Hiroshi Uemura, Nobutada Tanaka, Tatsuyshi Funasaka, Arayo Haga, Hisamitsu Nagase, Avraham Raz and Kazuo T. Nakamura
Affiliation:
Keywords: Crystallization, Motility Factor, cytokine
Abstract: Human autocrine motility factor (hAMF), a tumor-secreted cytokine which stimulates cell migration in vitro and metastasis in vivo, has been crystallized by the hanging-drop vapour diffusion method. The crystals belong to an orthorhombic space group P212121 with the cell dimensions of a = 80.79 A, b = 107.1 A, and c = 270.9 A. There are two dimers per asymmetric unit. The crystals diffract to at least 2.0 A resolution and are suitable for X-ray structure analysis at high resolution.
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Cite this article as:
Uemura Hiroshi, Tanaka Nobutada, Funasaka Tatsuyshi, Haga Arayo, Nagase Hisamitsu, Raz Avraham and Nakamura T. Kazuo, Crystallization and Preliminary X-Ray Crystallographic Studies of Human Autocrine Motility Factor, Protein & Peptide Letters 2001; 8 (4) . https://dx.doi.org/10.2174/0929866013409364
DOI https://dx.doi.org/10.2174/0929866013409364 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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