Purification, crystallization and preliminary X-ray analysis of human recombinant cytosolic serine hydroxymethyltransferase.
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.
Section of Structural Biology, Institute of Cancer Research, University of London, Cotswold Road, Sutton, Surrey SM2 5NG, England.
S B
SB
Renwick
J V
JV
Skelly
K J
KJ
Chave
P G
PG
Sanders
K
K
Snell
U
U
Baumann
D003460:Crystallization; D018360:Crystallography, X-Ray; D003600:Cytosol / Q000201:enzymology; D012696:Glycine Hydroxymethyltransferase / Q000737:chemistry* / Q000302:isolation & purification; D006801:Humans; D011487:Protein Conformation; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000302:isolation & purification
D011993:Recombinant Fusion Proteins; D012696:Glycine Hydroxymethyltransferase