Crystallization and preliminary crystallographic analysis of the extracellular fragment of FcalphaRI/CD89.
Crystals of the extracellular fragment of FcalphaRI/CD89 have been grown at 291 K using PEG 8000 as precipitant. The diffraction pattern of the selenomethionine (SeMet) derivative crystal extended to 2.1 A resolution at SPring-8, Japan. The crystals belong to space group C222(1), with unit-cell parameters a = 59.0, b = 69.4, c = 106.3 A, alpha = beta = gamma = 90 degrees. The presence of one molecule per asymmetric unit gives a crystal volume per protein mass (V(M)) of 3.12 A(3) Da(-1) and a solvent content of 60.2% by volume. A full set of X-ray diffraction data were collected to 2.1 A from an SeMet-derivative crystal.
Yang
Maojun
M
MOE Protein Science Laboratory and Laboratory of Structural Biology, Department of Biological Science and Biotechnology, Tsinghua University, Beijing 100084, People's Republic of China.
Xu
Gang
G
Li
Shentao
S
Sun
Lei
L
Shi
Ning
N
Zeng
Wenwen
W
Pang
Hai
H
Zhang
Wei
W
Rao
Zihe
Z
D015703:Antigens, CD / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000378:metabolism; D005110:Extracellular Space / Q000737:chemistry; D006801:Humans; D010446:Peptide Fragments / Q000737:chemistry*; D011961:Receptors, Fc / Q000737:chemistry*; D011994:Recombinant Proteins / Q000737:chemistry
D015703:Antigens, CD; C036832:Fc(alpha) receptor; D010446:Peptide Fragments; D011961:Receptors, Fc; D011994:Recombinant Proteins