Table 3.
Cross-linked proteins | Linkage sites | Ratio 1:50 | Ratio 1:100 | Distancea Cα–Cα (Å) |
---|---|---|---|---|
Bcd1pFL–Bcd1pFL | K16–K62 | √ | N.C. | |
K16–K88 | √ | √ | N.C. | |
K16–S106 | √ | N.C. | ||
K16–K109 | N.C. | |||
K16–K151 | √ | N.C. | ||
K16–K258 | √ | √ | N.C. | |
K62–K80 | √ | N.C. | ||
K80–K151 | √ | N.C. | ||
K87–K151 | √ | N.C. | ||
K140–K151 | √ | 15.4 | ||
K188–K151 | √ | √ | 10.1 | |
Rtt106p-M–Bcd1pFL | S177–K151 | √ | √ | 19.4 |
Identified cross-linked sites are represented for all tested ratios (technical duplicates).
aCα–Cα distances are indicated according to the crystal structure (N.C. for “not crystallized” mention is indicated for cross-links involving at least one site that has not been crystallized).