Work

Preliminary crystallographic investigations of glycinamide ribonucleotide transformylase

Year: 1989

Type: article

Abstract: Crystals of glycinamide ribonucleotide transformylase have been grown from 0.4 to 1 M ammonium sulfate, 0.6 to 1 M sodium-potassium phosphate, or 0.65 to 1 M citrate in the pH range 4.5-7.0. The single crystals display variable morphology with varying pH. The crystals belong to the orthorhombic space group C222 with cell dimensions a = 141.4 A, b = 98.2 A, c = 103.5 A. Co-crystals have also been obtained in the presence of the inhibitor 5,8-dideazafolate (KI = 18 microM) under similar crystallization conditions. Crystals of a chemically modified enzyme, iodinated at Cys-21, were grown under similar conditions within the pH range 6.5-7.0. These crystals are isomorphous with the unmodified enzyme. Crystals suitable for high resolution (less than 2.5 A) x-ray diffraction studies have been obtained for each of the above.

Source: Journal of Biological Chemistry

DOI: 10.1016/s0021-9258(18)60587-3

Authors: E A Stura, D L Johnson, J Inglese, J M Smith, S J Benkovic, I A Wilson

Institutions: Scripps Research Institute, Center for Infectious Disease Research, Pennsylvania State University, Scripps Clinic

Language: English

Topic: Enzyme Structure and Function

Subfield: Materials Chemistry

Field: Materials Science

Domain: Physical Sciences

Open Access status: hybrid

Estimated APC paid: $3,430

Funders: National Institute of General Medical Sciences, National Institute of Allergy and Infectious Diseases