Crystallization and preliminary crystallographic characterization of GTP cyclohydrolase I from Escherichia coli.
GTP cyclohydrolase I of Escherichia coli has been purified from a recombinant bacterial strain. The enzyme was crystallized from 0.6 M-sodium citrate and from 0.8 M-sodium/potassium phosphate, respectively. Crystals grown in citrate showed X-ray diffraction extending to a resolution better than 3 A. The space group was P2(1) with cell dimensions a = 204.8 A, b = 210.1 A, c = 72.2 A, alpha = gamma = 90 degrees and beta = 95.8 degrees.
Schmid
C
C
Lehrstuhl für Organische Chemie und Biochemie, Technische Universität München, Garching, Federal Republic of Germany.
Ladenstein
R
R
Luecke
H
H
Huber
R
R
Bacher
A
A
D001708:Biopterins / Q000031:analogs & derivatives / Q000096:biosynthesis; D003460:Crystallization; D004926:Escherichia coli / Q000201:enzymology*; D005492:Folic Acid / Q000031:analogs & derivatives / Q000096:biosynthesis; D006136:GTP Cyclohydrolase / Q000737:chemistry* / Q000302:isolation & purification; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry; D014961:X-Ray Diffraction
D011994:Recombinant Proteins; D001708:Biopterins; C010920:dihydrofolate; D005492:Folic Acid; D006136:GTP Cyclohydrolase; C003402:sapropterin