Taking MAD to the extreme: ultrafast protein structure determination

Multiwavelength anomalous diffraction data were measured in 23 min from a 16 kDa selenomethionyl‐substituted protein, producing experimental phases to 2.25 Å resolution. The data were collected on a mosaic 3 × 3 charge‐coupled device using undulator radiation from the Structural Biology Center 19ID...

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Bibliographic Details
Published in:Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 1999-06, Vol.55 (6), p.1168-1173
Main Authors: Walsh, Martin A., Dementieva, Irene, Evans, Gwyndaf, Sanishvili, Ruslan, Joachimiak, Andrzej
Format: Article
Language:English
Subjects:
ADVANCED PHOTON SOURCE
Base Sequence
BIOLOGY
Chaperonins - chemistry
CHARGE-COUPLED DEVICES
CRYSTAL STRUCTURE
DATA ACQUISITION
DIFFRACTION
DNA Primers
MAD
MATERIALS SCIENCE
PARTICLE ACCELERATORS
Protein Conformation
PROTEIN STRUCTURE
PROTEINS
RADIATIONS
Recombinant Proteins - chemistry
RESOLUTION
SYNCHROTRONS
Thermus thermophilus - chemistry
ultrafast structure determination
VELOCITY
WIGGLER MAGNETS
X-Ray Diffraction - methods
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Summary:Multiwavelength anomalous diffraction data were measured in 23 min from a 16 kDa selenomethionyl‐substituted protein, producing experimental phases to 2.25 Å resolution. The data were collected on a mosaic 3 × 3 charge‐coupled device using undulator radiation from the Structural Biology Center 19ID beamline at the Argonne National Laboratory's Advanced Photon Source. The phases were independently obtained semiautomatically by two crystallographic program suites, CCP4 and CNS. The quality and speed of this data acquisition exemplify the opportunities at third‐generation synchrotron sources for high‐throughput protein crystal structure deter­mination.
ISSN:1399-0047
0907-4449
1399-0047
DOI:10.1107/S0907444999003698