X-ray Laue diffraction from crystals of xylose isomerase.

AUTOR(ES)

Farber, G K

RESUMO

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.

Documentos Relacionados

• Thallium counterion distribution in cubic insulin crystals determined from anomalous x-ray diffraction data.
• X-ray diffraction studies of fibers and crystals of deoxygenated sickle cell hemoglobin.
• GROWTH, ORIENTATION, AND X-RAY DIFFRACTION OF SINGLE CRYSTALS NEAR LIQUID HELIUM TEMPERATURES
• Additional evidence from x-ray powder diffraction patterns that icosahedral quasi-crystals of intermetallic compounds are twinned cubic crystals
• X-ray diffraction of actively shortening muscle.