Crystallization and Preliminary X-Ray Crystallographic Studies of Human Autocrine Motility Factor
Authors: Uemura, H.; Tanaka, N.; Funasaka, T.; Haga, A.; Nagase, H.; Raz, A.; Nakamura, K.T.
Source: Protein and Peptide Letters, Volume 8, Number 4, August 2001 , pp. 317-322(6)
Publisher: Bentham Science Publishers
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.
Document Type: Review Article
Publication date: August 1, 2001
- Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.