Open AccessX-ray Laue diffraction from crystals of xylose isomerase.
Author(s) -
Gloria Färber,
P. A. Machin,
Steven C. Almo,
Gregory A. Petsko,
János Hajdu
Publication year - 1988
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.85.1.112
Subject(s) - diffractometer , monochromatic color , xylose isomerase , x ray crystallography , atom (system on chip) , crystal (programming language) , diffraction , crystallography , derivative (finance) , protein crystallization , millisecond , molecule , crystal structure , physics , chemistry , materials science , crystallization , isomerase , optics , nuclear magnetic resonance , computer science , enzyme , programming language , astronomy , financial economics , embedded system , economics , quantum mechanics , thermodynamics
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.
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