Crystallization and preliminary crystallographic characterization of GTP cyclohydrolase I from Escherichia coli

C Schmid; R Ladenstein; H Luecke; R Huber; A Bacher

doi:10.1016/0022-2836(92)91067-y

Crystallization and preliminary crystallographic characterization of GTP cyclohydrolase I from Escherichia coli

J Mol Biol. 1992 Aug 20;226(4):1279-81. doi: 10.1016/0022-2836(92)91067-y.

Authors

C Schmid¹, R Ladenstein, H Luecke, R Huber, A Bacher

Affiliation

¹ Lehrstuhl für Organische Chemie und Biochemie, Technische Universität München, Garching, Federal Republic of Germany.

PMID: 1518056
DOI: 10.1016/0022-2836(92)91067-y

Abstract

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Biopterins / analogs & derivatives
Biopterins / biosynthesis
Crystallization
Escherichia coli / enzymology*
Folic Acid / analogs & derivatives
Folic Acid / biosynthesis
GTP Cyclohydrolase / chemistry*
GTP Cyclohydrolase / isolation & purification
Recombinant Proteins / biosynthesis
Recombinant Proteins / chemistry
X-Ray Diffraction

Substances

Recombinant Proteins
Biopterins
dihydrofolate
Folic Acid
GTP Cyclohydrolase
sapropterin