Preliminary crystallographic analysis of a cruciferin protein from seeds of Moringa oleifera.
A 55 kDa cruciferin protein has been purified and characterized from seeds of Moringa oleifera plant. Protein blast of N-terminal amino-acid sequence showed 60 % sequence similarity with cruciferin from Brassica napus. The M. oleifera protein has been crystallized applying the sitting drop method using 5 % polyethylene glycol 8,000, 38.5 % 3-methyl-1,5-pentanediol and 0.1 M sodium cacodylate pH 6.5. The crystals belonged to the P6322 hexagonal space group with cell dimensions, a = b = 98.4, c = 274.3 Å. Initial diffraction data have been collected to a resolution of 6 Å.
Laboratory for Structural Biology of Infection and Inflammation, Department of Chemistry, c/o DESY, University of Hamburg, Notkestrasse 85, 22603, Hamburg, Germany, ahmedakrem@hotmail.com.
Ahmed
A
Akrem
Nasser
N
Yousef
Afshan
A
Begum
Amr
A
Negm
Arne
A
Meyer
Markus
M
Perbandt
Friedrich
F
Buck
Christian
C
Betzel
D029688:Brassica napus; D003461:Crystallography / Q000379:methods*; D029588:Moringa oleifera / Q000737:chemistry*; D055314:Seed Storage Proteins / Q000737:chemistry*; D012639:Seeds / Q000737:chemistry*
D055314:Seed Storage Proteins