Title

Crystallization of human thymidylate synthase

UMMS Affiliation

Department of Biochemistry and Molecular Pharmacology

Publication Date

1991-05-20

Document Type

Article

Subjects

Cloning, Molecular; Crystallization; Escherichia coli; Humans; Protein Conformation; Recombinant Proteins; Thymidylate Synthase; X-Ray Diffraction

Disciplines

Biochemistry, Biophysics, and Structural Biology | Pharmacology, Toxicology and Environmental Health

Abstract

Human thymidylate synthase has been crystallized in the absence of ligands and diffracts beyond 3.0 A. The protein was cloned and expressed in Escherichia coli and then crystallized from ammonium sulfate in the presence of beta-mercaptoethanol at a variety of pH values. The crystals are trigonal in the space-group P3(1)21; the unit cell dimensions are a = b = 96.7 A, c = 84.1 A.

Source

J Mol Biol. 1991 May 20;219(2):161-3.

Journal/Book/Conference Title

Journal of molecular biology

Related Resources

Link to Article in PubMed

PubMed ID

2038053

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