Crystallization and preliminary crystallographic studies of L30e, a ribosomal protein from Methanocaldococcus jannaschii (MJ1044).
In view of the biological significance of understanding the ribosomal machinery of both prokaryotes and eukaryotes, the L30e ribosomal protein from Methanocaldococcus jannaschii was cloned, overexpressed, purified and crystallized using the microbatch-under-oil method with the crystallization conditions 40% PEG 400, 0.1 M MES pH 6.0 and 5% PEG 3000 at 291 K. A diffraction-quality crystal (0.20 x 0.20 x 0.35 mm) was obtained that belonged to the primitive tetragonal space group P4(3), with unit-cell parameters a = 46.1, b = 46.1, c = 98.5 A, and diffracted to a resolution of 1.9 A. Preliminary calculations reveal that the asymmetric unit contains two monomers with a Matthews coefficient (V(M)) of 2.16 A(3) Da(-1).
Rangarajan
Sarani
S
Bioinformatics Centre, Indian Institute of Science, Bangalore 560 012, India.
Jeyakanthan
Jeyaraman
J
Mridula
Palappetty
P
Sakamoto
Keiko
K
Kitamura
Yoshiaki
Y
Agari
Yoshihiro
Y
Shinkai
Akeo
A
Ebihara
Akio
A
Kuramitsu
Seiki
S
Yokoyama
Shigeyuki
S
Sekar
Kanagaraj
K
D001483:Base Sequence; D003460:Crystallization; D018360:Crystallography, X-Ray; D017931:DNA Primers; D017016:Methanococcaceae / Q000737:chemistry*; D016133:Polymerase Chain Reaction; D012269:Ribosomal Proteins / Q000737:chemistry*
D017931:DNA Primers; D012269:Ribosomal Proteins; C035201:ribosomal protein L30