Crystallization and preliminary X-ray analysis of class II fructose-1,6-bisphosphate aldolase from Thermus caldophilus.
In this study, we have crystallized class II fructose-1,6-bisphosphate aldolase (FBA) from Thermus caldophilus (Tca). Purified Tca FBA is a tetrameric enzyme of 305 residues, which crystallizes in the space group P2(1)2(1)2(1) (cell dimensions a = 98.9, b = 113.1, c = 115.7 A), with four molecules in the asymmetric unit. A complete diffraction data set was obtained from orthorhombic crystals at resolution of 2.2 A.
Lee
Jun Hyuck
JH
Department of Life Science, Kwangju Institute of Science & Technology, Gwangju 500-712, Korea.
Im
Young Jun
YJ
Rho
Seong-Hwan
SH
Park
Seong Ho
SH
Kim
Mun-Kyoung
MK
Cho
Su Jin
SJ
Kim
Tae-Yeon
TY
Oh
Jin Hwan
JH
Shin
Hyun-Jae
HJ
Lee
Dae-Sil
DS
Eom
Soo Hyun
SH
D000595:Amino Acid Sequence; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000706:statistics & numerical data; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D005634:Fructose-Bisphosphate Aldolase / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D008969:Molecular Sequence Data; D011994:Recombinant Proteins / Q000737:chemistry; D016415:Sequence Alignment; D013824:Thermus / Q000201:enzymology*
D011994:Recombinant Proteins; D005634:Fructose-Bisphosphate Aldolase