Abstract
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.
Original language | English (US) |
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Pages (from-to) | 112-115 |
Number of pages | 4 |
Journal | Proceedings of the National Academy of Sciences of the United States of America |
Volume | 85 |
Issue number | 1 |
DOIs | |
State | Published - Jan 1988 |
Externally published | Yes |
ASJC Scopus subject areas
- General