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Updated: Aug 11, 2026
Thermostabilization, Expression, Purification, and Crystallization of the Human Serotonin Transporter Bound to S-citalopram
Published on: November 27, 2016
Purification, crystallization and preliminary X-ray analysis of human recombinant cytosolic serine
S B Renwick1, J V Skelly, K J Chave
1Section of Structural Biology, Institute of Cancer Research, University of London, Cotswold Road, Sutton, Surrey SM2 5NG, England.
Abstract:
As an enzyme of the thymidylate synthase cycle, serine hydroxymethyltransferase (SHMT) has a key role in nucleotide biosynthesis. Elevated activities of SHMT have been correlated with the increased demand for nucleotide biosynthesis in tumors of human and rodent origin, making this enzyme a novel target for cancer chemotherapy. Here the purification and crystallization of recombinant human cytosolic SHMT are reported. Crystals belong to space group P6222 or P6422 with cell parameters a = b = 155.0, c = 235.5 A and diffract to at least 3.0 A resolution.
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