Protein microcrystal diffraction and the effects of radiation damage with ultra-high-flux synchrotron radiation.
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.
B
B
Hedman
K O
KO
Hodgson
J R
JR
Helliwell
R
R
Liddington
M Z
MZ
Papiz
D006096:Gramicidin; D010315:Particle Accelerators; D011506:Proteins / Q000528:radiation effects; D014961:X-Ray Diffraction / Q000379:methods*
D011506:Proteins; D006096:Gramicidin