Crystallization and preliminary X-ray investigation of Escherichia coli porphobilinogen deaminase.
Porphobilinogen deaminase, the polymerase that catalyses the synthesis of preuroporphyrinogen, the linear tetrapyrrole precursor of uroporphyrinogen III, has been crystallized from sodium acetate buffer with polyethylene glycol 6000 as precipitant. The crystals are orthorhombic and the space group is P2(1)2(1)2, with unit cell dimensions a = 88.01 A, b = 75.86 A, c = 50.53 A and alpha = beta = gamma = 90 degrees, indicating a single molecule of 34 kDa in the asymmetric unit. The crystals grow to dimensions of 1 mm x 2 mm x 0.5 mm within two weeks in the dark and are stable in the X-ray beam for at least 40 hours. Diffraction data beyond 1.7 A resolution, observed with a synchrotron radiation source, indicate that a high resolution structure analysis is feasible.
Jordan
P M
PM
School of Biological Sciences, Queen Mary and Westfield College, London, U.K.
Warren
M J
MJ
Mgbeje
B I
BI
Wood
S P
SP
Cooper
J B
JB
Louie
G
G
Brownlie
P
P
Lambert
R
R
Blundell
T L
TL
D003460:Crystallization; D004926:Escherichia coli / Q000201:enzymology*; D011163:Hydroxymethylbilane Synthase / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D015394:Molecular Structure; D014961:X-Ray Diffraction
D011163:Hydroxymethylbilane Synthase