Crystallization and preliminary X-ray diffraction studies of dialkylglycine decarboxylase, a decarboxylating transaminase.
The pyridoxal phosphate-dependent enzyme dialkylglycine decarboxylase (E.C. 4.1.1.64) has been crystallized by vapor diffusion from a 15% polyethyleneglycol solution with sodium pyruvate as coprecipitant. The space group of the crystals is either P6(2)22 or the enantiomorph, P6(4)22, with one subunit of 46,500 Da per asymmetric unit. The unit cell has dimensions a = b = 152.7 A, c = 86.6 A, alpha = beta = 90 degrees, gamma = 120 degrees, and a solvent content of approximately 61%. diffraction extends to 2.3 A resolution.
Toney
M D
MD
Department of Structural Biology, University of Basel, Switzerland.
Keller
J W
JW
Pauptit
R A
RA
Jaeger
J
J
Wise
M K
MK
Sauder
U
U
Jansonius
J N
JN
D016956:Burkholderia cepacia / Q000201:enzymology*; D002262:Carboxy-Lyases / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D003460:Crystallization; D046911:Macromolecular Substances; D011487:Protein Conformation; D011732:Pyridoxal Phosphate / Q000378:metabolism; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D014961:X-Ray Diffraction
D046911:Macromolecular Substances; D011994:Recombinant Proteins; D011732:Pyridoxal Phosphate; D002262:Carboxy-Lyases; C063519:2,2-dialkylglycine decarboxylase