Preliminary X-ray Crystallography Studies of Recombinant Human Interleukin-1α
Year: 1989
Type: article
Abstract: Human interleukin-1 alpha, cloned and expressed in E. coli, has been purified and structurally characterized by various physiochemical methods, including mass spectrometry. The recombinant protein has been crystallized by the hanging drop vapor diffusion method using dimethyl sulfoxide as the precipitating agent. The space group is P2(1)2(1)2(1). Unit cell dimensions are a = 44.1, b = 57.1, and c = 61.7 A and alpha = beta = gamma = 90 degrees. The crystals diffract to beyond 1.7 A and are suitable for high resolution data collection. Native diffraction data were collected. Screens for heavy atom derivatives have been initiated.
Source: Journal of Biological Chemistry
Authors: A M Hassell, K O Johanson, P Goodhart, P R Young, B P Holskin, S A Carr, G D Roberts, P L Simon, M J Chen, M Lewis
Language: English
Subfield: Materials Chemistry
Field: Materials Science
Domain: Physical Sciences
Open Access status: hybrid
Estimated APC paid: $3,430
OpenAlex ID: W1594572460