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J. Biochem, 1988, Vol. 104, No. 5 679-680
© 1988 Japanese Biochemical Society

other

Crystallization and Preliminary X-Ray Data for 3-Isopropylmalate Dehydrogenase of Thermus thermophilus1

Yukiteru Katsube*, Nobuo Tanaka**,2, Akio Takenaka**, Tairo Oshima** and Tohru Yamada**

*Institute of Protein Research, Osaka University Suita, Osaka 565
**Department of Life Science, Faculty of Science, Tokyo Institute of Technology Midori-ku, Yokohama, Kanagawa 227

2 To whom correspondence should be addressed

The gene coding for 3-isopropylmalate dehydrogenase of Thermus thermophilus was cloned and expressed in Escherichia coli. The extracted enzyme was crystallized in a suitable size for X-ray crystallographic studies. The crystals have a space group of P3121 or P3221 with a = b = 78.6 Å and c = 157.4 Å.

1 This study was supported in part by a Grant-in-Aid for Scientific Research (60-4) from the Ministry of Education, Science and Culture of Japan (Nos. 60060004, 61304062, 63111001, and 63111005).


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