X-ray Laue diffraction from crystals of xylose isomerase.

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

Research output: Contribution to journalArticle

35 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)112-115
Number of pages4
JournalProceedings of the National Academy of Sciences of the United States of America
Volume85
Issue number1
StatePublished - Jan 1988
Externally publishedYes

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xylose isomerase
X-Ray Diffraction
X-Rays
Catalytic Domain
Proteins

ASJC Scopus subject areas

  • General
  • Genetics

Cite this

X-ray Laue diffraction from crystals of xylose isomerase. / Farber, G. K.; Machin, P.; Almo, Steven C.; Petsko, G. A.; Hajdu, J.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 85, No. 1, 01.1988, p. 112-115.

Research output: Contribution to journalArticle

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