Crystallization and preliminary X-ray diffraction studies of a flavoprotein, FP390, from a luminescent bacterium, Photobacterium phosphoreum.
A flavoprotein, FP390, obtained from a luminescent bacterium, Photobacterium phosphoreum, in the purification of luciferase has been crystallized by the vapor-diffusion procedure. Crystals obtained from polyethylene glycol 4000 solutions, whose X-ray photographs show powder diffraction patterns, were unsuitable for further crystallographic work. However, tetragonal crystals grown from potassium phosphate solution well diffracted X-rays beyond 3 A resolution. The space group of this crystal is P4(1)22 or P4(3)22 with unit-cell dimensions of a = b = 76.8 and c = 241 A. Assuming two or three molecules in an asymmetric unit, the value for the crystal volume per unit molecular mass, Vm, is calculated as 3.3 or 2.2 A3/Da, respectively. A total of 13,555 independent reflections for the native crystal was collected up to 3 A resolution using a Weissenberg camera attached to the synchrotron radiation source, the merging R factor being 0.077 for 79,335 measurements.
Kita
A
A
Department of Applied Chemistry, Faculty of Engineering, Osaka University.
Kasai
N
N
Kasai
S
S
Nakaya
T
T
Miki
K
K
D001426:Bacterial Proteins / Q000737:chemistry / Q000302:isolation & purification*; D005420:Flavoproteins / Q000737:chemistry / Q000302:isolation & purification*; D008163:Luminescent Measurements; D010776:Photobacterium / Q000737:chemistry*; D011487:Protein Conformation; D014961:X-Ray Diffraction
D001426:Bacterial Proteins; D005420:Flavoproteins