Crystallization and X-ray analysis of a single fab binding domain from protein L of Peptostreptococcus magnus.
Protein L is a multidomain cell wall constituent of certain strains of Peptostreptococcus magnus which binds to the variable domain of immunoglobulin kappa-light chains. A single immunoglobulin-binding domain of M(r) = 9000 from this protein has been isolated and crystallized. The crystals are of space group P4(2)2(1)2, with cell dimensions a = b = 66.9 A, c = 68.3 A, and diffract to at least 2.2 A resolution. The asymmetric unit of the crystal contains two molecules of the protein L domain, related by a noncrystallographic 2-fold axis, as revealed by a self-rotation function calculated with native diffraction data.
Sohi
M K
MK
Biomedical Sciences Division, King's College London, UK.
Wan
T
T
Sutton
B J
BJ
Atkinson
T
T
Atkinson
M A
MA
Murphy
J P
JP
Bottomley
S P
SP
Gore
M G
MG
D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D001666:Binding Sites, Antibody; D002473:Cell Wall / Q000378:metabolism; D003460:Crystallization; D018360:Crystallography, X-Ray; D006801:Humans; D007140:Immunoglobulin Fab Fragments / Q000378:metabolism*; D008970:Molecular Weight; D010462:Peptostreptococcus / Q000378:metabolism*; D011487:Protein Conformation
D001426:Bacterial Proteins; C055047:Ig L-binding protein, Peptostreptococcus; D007140:Immunoglobulin Fab Fragments