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Updated: Oct 24, 2026

Crystallization and Structural Determination of an Enzyme:Substrate Complex by Serial Crystallography in a Versatile Microfluidic Chip
Published on: March 20, 2021
Crystallization and preliminary X-ray analysis of the unliganded recombinant catalytic subunit of cAMP-dependent
N Narayana1, P Akamine, N H Xuong
1Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA 92093-0359, USA.
Abstract:
X-ray diffraction-quality crystals of the unliganded mouse recombinant catalytic subunit of cAMP-dependent protein kinase were grown by the hanging-drop vapour-diffusion technique using 2-methyl-2,4-pentanediol as precipitant. The crystals belong to the monoclinic space group P21 with unit-cell parameters a = 48.9, b = 147.4, c = 54.2 A, beta = 110.2 degrees. A data set to 3.0 A resolution with 92% completeness has been collected using synchrotron radiation. The unit cell contains four molecules of molecular weight 40 kDa with a corresponding volume solvent content of 45%.

