Crystallization and preliminary X-ray crystallographic studies of recombinant human leukotriene A4 hydrolase complexed with bestatin.
Recombinant human leukotriene A4 hydrolase complexed with bestatin, an inhibitor of metalloprotease, has been crystallized by the hanging drop vapor diffusion method using 0.1 M phosphate buffer (pH 6.5) and 50 to 54% saturated ammonium sulfate. The orthorhombic crystals belong to the space group I222 or I2(1)2(1)2(1) with unit cell dimensions of a = 273.6 A, b = 261.3 A and c = 52.9 A. They diffract beyond 2.5 A resolution and a native data set up to 3 A resolution has been collected on an imaging plate Weissenberg camera using synchrotron radiation.
Tsuge
H
H
Life Science Research Laboratory, Japan Tobacco, Inc., Kanagawa.
Ago
H
H
Aoki
M
M
Furuno
M
M
Noma
M
M
Miyano
M
M
Minami
M
M
Izumi
T
T
Shimizu
T
T
D000595:Amino Acid Sequence; D003460:Crystallization; D018360:Crystallography, X-Ray; D004851:Epoxide Hydrolases / Q000737:chemistry*; D006801:Humans; D007930:Leucine / Q000031:analogs & derivatives* / Q000737:chemistry; D008969:Molecular Sequence Data; D015394:Molecular Structure; D011480:Protease Inhibitors / Q000737:chemistry*; D011994:Recombinant Proteins / Q000737:chemistry
D011480:Protease Inhibitors; D011994:Recombinant Proteins; D004851:Epoxide Hydrolases; D007930:Leucine; C012211:ubenimex; C043134:leukotriene A4 hydrolase