Crystallization and preliminary X-ray diffraction analysis of the cytosolic domain of a cation diffusion facilitator family protein
Related Experiment Video
Updated: Jul 12, 2026

Crystallization and Structural Determination of an Enzyme:Substrate Complex by Serial Crystallography in a Versatile Microfluidic Chip
Published on: March 20, 2021
Motoyuki Hattori1, Yoshiki Tanaka, Ryuichiro Ishitani
1Department of Biological Information, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, 4259 Nagatsuta-cho, Midori-ku, Yokohama-shi, Kanagawa 226-8501, Japan.
Abstract:
The cation diffusion facilitator (CDF) family proteins are ubiquitously distributed in the three domains of life and transport metals such as zinc and various heavy metals. Prokaryotic CDF proteins consists of an N-terminal putative six-transmembrane domain followed by a C-terminal cytosolic domain. The cytosolic domain of the CDF-family protein from Thermotoga maritima has been overexpressed, purified and crystallized. The selenomethionine-substituted crystals diffracted X-rays to 2.5 A resolution using synchrotron radiation, belonged to space group R32, with unit-cell parameters a = b = 97.7, c = 83.4 A, and are expected to contain one molecule in each asymmetric unit.

