Figure 2.
Fig 2. Structure and conformation of CD21 SCR1-SCR2. (A)
Ribbon drawing of the crystallized protein, with -strands
labeled. Disulfide bonds and NAG residues are shown in yellow
and orange, respectively. (B) Interface between domains SCR1 and
SCR2. Amino acids (single-letter code) that participate in the
contact are shown in green. Hydrogen bonds and salt bridges are
represented with dashed lines. A comparison with the structure
of liganded CD21 SCR1-SCR2 (gray) (17) reveals substantial
interdomain flexibility despite extensive interface contacts.
(C) Final 2 F[obs] - F[calc] electron density map at 1.8-Å
resolution, contoured at 0.7 , and centered at NAG107.
-strands
labeled. Disulfide bonds and NAG residues are shown in yellow
and orange, respectively. (B) Interface between domains SCR1 and
SCR2. Amino acids (single-letter code) that participate in the
contact are shown in green. Hydrogen bonds and salt bridges are
represented with dashed lines. A comparison with the structure
of liganded CD21 SCR1-SCR2 (gray) (17) reveals substantial
interdomain flexibility despite extensive interface contacts.
(C) Final 2 F[obs] - F[calc] electron density map at 1.8-Å
resolution, contoured at 0.7 
, and centered at NAG107.