Open AccessProtein microcrystal diffraction and the effects of radiation damage with ultra-high-flux synchrotron radiation.
Author(s) -
Britt Hedman,
Keith O. Hodgson,
John R. Helliwell,
R.C. Liddington,
Miroslav Z. Papiz
Publication year - 1985
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.82.22.7604
Subject(s) - synchrotron radiation , wiggler , protein crystallization , synchrotron , diffraction , flux (metallurgy) , radiation , optics , radiation damage , x ray crystallography , reciprocal lattice , materials science , crystal (programming language) , physics , crystallography , chemistry , nuclear physics , crystallization , cathode ray , computer science , metallurgy , thermodynamics , programming language , electron
By using ultra-high-flux synchrotron x-radiation from a wiggler source, good Laue diffraction data have been obtained from protein microcrystals of size 30 X 35 X 10 microns3, mounted wet in glass capillaries. At the flux level of 10(13)-10(14) photons per sec/mm2, the radiation damage is still low enough to allow a large survey of reciprocal space for a microcrystal and a complete survey for a normal-sized protein crystal. The development of sources for ultra-high-intensity synchrotron radiation is thus an important improvement in the technique for determination of structure through protein crystallography as well as in other cases where crystal size is often a limiting factor.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom