Abstract:
:The emerging method of femtosecond crystallography (FX) may extend the diffraction resolution accessible from small radiation-sensitive crystals and provides a means to determine catalytically accurate structures of acutely radiation-sensitive metalloenzymes. Automated goniometer-based instrumentation developed for use at the Linac Coherent Light Source enabled efficient and flexible FX experiments to be performed on a variety of sample types. In the case of rod-shaped Cpl hydrogenase crystals, only five crystals and about 30 min of beam time were used to obtain the 125 still diffraction patterns used to produce a 1.6-Å resolution electron density map. For smaller crystals, high-density grids were used to increase sample throughput; 930 myoglobin crystals mounted at random orientation inside 32 grids were exposed, demonstrating the utility of this approach. Screening results from cryocooled crystals of β2-adrenoreceptor and an RNA polymerase II complex indicate the potential to extend the diffraction resolution obtainable from very radiation-sensitive samples beyond that possible with undulator-based synchrotron sources.
journal_name
Proc Natl Acad Sci U S Aauthors
Cohen AE,Soltis SM,González A,Aguila L,Alonso-Mori R,Barnes CO,Baxter EL,Brehmer W,Brewster AS,Brunger AT,Calero G,Chang JF,Chollet M,Ehrensberger P,Eriksson TL,Feng Y,Hattne J,Hedman B,Hollenbeck M,Holton JM,Keabdoi
10.1073/pnas.1418733111subject
Has Abstractpub_date
2014-12-02 00:00:00pages
17122-7issue
48eissn
0027-8424issn
1091-6490pii
1418733111journal_volume
111pub_type
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