Crystallization and preliminary X-ray analysis of eukaryotic initiation factor 4E from Pisum sativum.
Crystals of an N-terminally truncated 20 kDa fragment of Pisum sativum eIF4E (DeltaN-eIF4E) were grown by vapour diffusion. X-ray data were recorded to a resolution of 2.2 A from a single crystal in-house. Indexing was consistent with primitive monoclinic symmetry and solvent-content estimations suggested that between four and nine copies of the eIF4E fragment were possible per crystallographic asymmetric unit. eIF4E is an essential component of the eukaryotic translation machinery and recent studies have shown that point mutations of plant eIF4Es can confer resistance to potyvirus infection.
Ashby
Jamie A
JA
Department of Disease and Stress Biology, John Innes Centre, Norwich NR4 7UH, England.
Stevenson
Clare E M
CE
Maule
Andrew J
AJ
Lawson
David M
DM
D003460:Crystallization; D018360:Crystallography, X-Ray; D039561:Eukaryotic Initiation Factor-4E / Q000737:chemistry* / Q000302:isolation & purification; D018532:Pisum sativum / Q000737:chemistry*; D011487:Protein Conformation
D039561:Eukaryotic Initiation Factor-4E