TY - JOUR
T1 - Maltodextrin-dependent Crystallization of Cyclomaltodextrin Glucanotransferase from Bacillus circulans
AU - Lawson, Catherine L.
AU - Bergsma, Jack
AU - Bruinenberg, Peter M.
AU - Vries, Gert de
AU - Dijkhuizen, Lubbert
AU - Dijkstra, Bauke W.
N1 - Relation: http://www.rug.nl/gbb/
date_submitted:2009
Rights: University of Groningen, Groningen Biomolecular Sciences and Biotechnology Institute
PY - 1990/8/20
Y1 - 1990/8/20
N2 - Crystals of cyclomaltodextrin glucanotransferase from Bacillus circulans (EC 2.4.1.19) suitable for high-resolution X-ray analysis were obtained by vapor diffusion against 60% (v/v) 2-methyl 2,4-pentanediol buffered with 100 mM-sodium Hepes, pH 7.55. The crystals have P212121 space group symmetry, with a=120.4 Å, b=110.9 Å and c=66.4 Å, and contain one molecule of 68,000 in the asymmetric unit. Growth of single enzyme crystals was found to require the presence of either α-cyclodextrin, β-cyclodextrin, γ-cyclodextrin, or maltose in high molar excess, a requirement that could not be fulfilled by glucose, the basic building block of these compounds. Although the exact role of cyclic and linear maltodextrins in enzyme crystallization is not yet known, we have preliminary evidence that these compounds are degraded by the enzyme in the crystallization droplet.
AB - Crystals of cyclomaltodextrin glucanotransferase from Bacillus circulans (EC 2.4.1.19) suitable for high-resolution X-ray analysis were obtained by vapor diffusion against 60% (v/v) 2-methyl 2,4-pentanediol buffered with 100 mM-sodium Hepes, pH 7.55. The crystals have P212121 space group symmetry, with a=120.4 Å, b=110.9 Å and c=66.4 Å, and contain one molecule of 68,000 in the asymmetric unit. Growth of single enzyme crystals was found to require the presence of either α-cyclodextrin, β-cyclodextrin, γ-cyclodextrin, or maltose in high molar excess, a requirement that could not be fulfilled by glucose, the basic building block of these compounds. Although the exact role of cyclic and linear maltodextrins in enzyme crystallization is not yet known, we have preliminary evidence that these compounds are degraded by the enzyme in the crystallization droplet.
U2 - 10.1016/0022-2836(90)90335-J
DO - 10.1016/0022-2836(90)90335-J
M3 - Article
SN - 0022-2836
VL - 214
SP - 807
EP - 809
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
IS - 4
ER -