Crystallization and preliminary X-ray diffraction studies of the human erythrocyte bisphosphoglycerate mutase

Crystallization and preliminary X-ray diffraction studies of the human erythrocyte bisphosphoglycerate mutase

Bisphosphoglycerate mutase (EC 2.7.5.4) catalyzes the synthesis and breakdown of 2,3-diphosphoglycerate in red cells. The human enzyme, cloned and expressed in Escherichia coli has been crystallized in the rhombohedral space group R32 with a = b = c = 100.4 A and alpha = beta = gamma = 81.2 degrees....

Full description

Saved in:
Bibliographic Details
Published in:Journal of molecular biology Vol. 218; no. 2; p. 269
Main Authors: Cherfils, J, Rosa, R, Garel, M C, Calvin, M C, Rosa, J, Janin, J
Format: Journal Article
Language:English
Published: England 20-03-1991
Subjects:
Bisphosphoglycerate Mutase - chemistry
Bisphosphoglycerate Mutase - genetics
Bisphosphoglycerate Mutase - metabolism
Cloning, Molecular
Crystallization
Erythrocytes - enzymology
Escherichia coli - genetics
Gene Expression
Humans
X-Ray Diffraction
Online Access:Get more information
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Bisphosphoglycerate mutase (EC 2.7.5.4) catalyzes the synthesis and breakdown of 2,3-diphosphoglycerate in red cells. The human enzyme, cloned and expressed in Escherichia coli has been crystallized in the rhombohedral space group R32 with a = b = c = 100.4 A and alpha = beta = gamma = 81.2 degrees. The asymmetric unit contains either a dimeric enzyme molecule, or a monomer.
ISSN:0022-2836
DOI:10.1016/0022-2836(91)90710-N