X-ray Laue diffraction from crystals of xylose isomerase.

G. K. Farber, P. Machin, S. C. Almo, G. A. Petsko, J. Hajdu

Research output: Contribution to journalArticlepeer-review

36 Scopus citations


The Laue method (stationary crystal, polychromatic x-rays) was used to collect native and heavy-atom-derivative data on crystals of xylose isomerase (EC 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 languageEnglish (US)
Pages (from-to)112-115
Number of pages4
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number1
StatePublished - Jan 1988
Externally publishedYes

ASJC Scopus subject areas

  • General


Dive into the research topics of 'X-ray Laue diffraction from crystals of xylose isomerase.'. Together they form a unique fingerprint.

Cite this