Crystallization and preliminary x-ray investigation of the regulatory subunit of cAMP-dependent protein kinase

• Published in: The Journal of biological chemistry Vol. 260; no. 16; pp. 9380 - 9381
• Main Authors: Lee, J H, Bechtel, P J, Phillips, G N
• Format: Journal Article
• Language: English
• Published: Bethesda, MD Elsevier Inc 05-08-1985; American Society for Biochemistry and Molecular Biology
• Subjects: Animals; Biological and medical sciences; Cattle; Crystalline structure; Crystallization; Cyclic AMP - metabolism; Fundamental and applied biological sciences. Psychology; Molecular biophysics; Muscles - enzymology; Protein Conformation; Protein Kinases - isolation & purification; Protein Kinases - metabolism; Structure in molecular biology; X-Ray Diffraction - methods; Bovine; Protein kinase; Animal; Crystallization; Dependence; AMP-3',5'; Striated muscle; X ray diffraction; Crystalline structure
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1016/S0021-9258(17)39375-4

Crystals of type I cAMP-dependent protein kinase regulatory subunit have been grown from solutions of ammonium sulfate. The crystals are square bipyramids, space group P4(1)2(1)2 (P4(3)2(1)2), with a = b = 106.9 +/- 0.6 A and c = 212.4 +/- 1.0 A. There are two dimers of the regulatory subunit/crystallographic asymmetric unit. The crystals are stable for 3-4 days in the x-ray beam and diffract to at least 3.5-A resolution.