Crystallization and preliminary crystallographic studies of a ribosomal protein L30e from the hyperthermophilic archaeon Thermococcus celer.
Ribosomal protein L30e from the hyperthermophilic archaeon Thermococcus celer is a good model for the study of the thermostability of proteins. It has been overexpressed, purified and crystallized using the hanging-drop vapour-diffusion method using PEG 8000 as precipitant at 290 K. The crystal belongs to the hexagonal space group P6(1)/P6(5), with unit-cell parameters a = b = 48.32, c = 86.42 A. The asymmetric unit contains a single molecule of L30e, with a corresponding crystal volume per protein mass (V(M)) of 2.68 A(3) Da(-1) and a solvent content of 54%. A complete data set diffracting to 1.96 A resolution was collected from a single crystal at 100 K.
Wong
K B
KB
Department of Biochemistry, The Chinese University of Hong Kong, Shatin, Hong Kong. kbwong@cuhk.edu.hk
Wang
W K
WK
Proctor
M R
MR
Bycroft
M
M
Chen
Y W
YW
D019843:Archaeal Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D011487:Protein Conformation; D012269:Ribosomal Proteins / Q000737:chemistry*; D019712:Thermococcus / Q000737:chemistry*
D019843:Archaeal Proteins; D012269:Ribosomal Proteins; C035201:ribosomal protein L30