PURIFICATION, CRYSTALLIZATION AND PRELIMINARY-X-RAY ANALYSIS OF HUMANRECOMBINANT CYTOSOLIC SERINE HYDROXYMETHYLTRANSFERASE

Authors
RENWICK SB SKELLY JV CHAVE KJ SANDERS PG SNELL K BAUMANN U
Citation
Sb. Renwick et al., PURIFICATION, CRYSTALLIZATION AND PRELIMINARY-X-RAY ANALYSIS OF HUMANRECOMBINANT CYTOSOLIC SERINE HYDROXYMETHYLTRANSFERASE, Acta crystallographica. Section D, Biological crystallography, 54, 1998, pp. 1030-1031
Citations number
17
Categorie Soggetti
Crystallography,"Biochemical Research Methods",Biophysics,Biology
Journal title
Acta crystallographica. Section D, Biological crystallography → ACNP
ISSN journal
09074449
Volume
54
Year of publication
1998
Part
5
Pages
1030 - 1031
Database
ISI
SICI code
0907-4449(1998)54:<1030:PCAPAO>2.0.ZU;2-S
Abstract
As an enzyme of the thymidylate synthase cycle, serine hydroxymethyltr ansferase (SHMT) has a key role in nucleotide biosynthesis. Elevated a ctivities of SHMT have been correlated with the increased demand for n ucleotide biosynthesis in tumors of human and rodent origin, making th is enzyme a novel target for cancer chemotherapy. Here the purificatio n and crystallization of recombinant human cytosolic SHMT are reported . Crystals belong to space group P6(2)22 or P6422 with cell parameters a = b = 155.0, c = 235.5 Angstrom and diffract to at least 3.0 Angstr om resolution.