X-ray Laue diffraction from crystals of xylose isomerase.
The Laue method (stationary crystal, polychromatic x-rays) was used to collect native and heavy-atom-derivative data on crystals of xylose isomerase (EC 5.3.1.5). These data were used to find the heavy-atom positions. The positions found by use of Laue data are the same as those found by use of monochromatic data collected on a diffractometer. These results confirm that Laue diffraction data sets, which can be obtained on a millisecond time scale, can be used to locate small molecules bound to protein active sites. The successful determination of heavy-atom positions also indicates that x-ray crystallographic data collected by the Laue method can be used to solve protein structures.
Farber
G K
GK
Department of Chemistry, Massachusetts Institute of Technology, Cambridge 02139.
Machin
P
P
Almo
S C
SC
Petsko
G A
GA
Hajdu
J
J
D019747:Aldose-Ketose Isomerases; D002238:Carbohydrate Epimerases; D008958:Models, Molecular; D011487:Protein Conformation; D014961:X-Ray Diffraction / Q000379:methods
D002238:Carbohydrate Epimerases; D019747:Aldose-Ketose Isomerases; C023298:xylose isomerase