Table II. Crystallographic data and refinement statistics.
| Sel-α3GalT | Sel-α3GalT | Sel-α3GalT | α3GalT | α3GalT + UDPG | |
|---|---|---|---|---|---|
| Wavelength (Å) | 0.9796 | 0.9800 | 0.9324 | 0.9324 | 0.9324 |
| Peak (W1) | inflection (W2) | remote (W3) | |||
| Energy (Kev) | 12.6566 | 12.6515 | 13.2971 | 13.2971 | 13.271 |
| Resolution (Å) | 30.0–2.8 | 30.0–2.8 | 30.0–2.8 | 30.0–2.0 | 30.0–2.5 |
| Unit cell, a = b, c (Å) | 95.55, 112.71 | 95.55, 112.71 | 95.55, 112.71 | 95.56, 112.71 | 95.6, 110.72 |
| No. of unique reflections | 10 366 | 10 366 | 10 366 | 31 286 | 18 010 |
| [I/σ(I)] | 5.7 (1.8) | 5.6 (2.0) | 7.2 (1.7) | 7.5 (1.8) | 9.3 (2.4) |
| Rsym (%)a | 7.9 (20) | 7.7 (19.5) | 7.5 (12) | 5.8 (38.3) | 4.3 (22.7) |
| Ranomal (%) | 8.0 (15.5) | 5.9 (13.2) | 6.7 (9.5) | ||
| Completeness (%) | 97.6 (97.6) | 98.2 (98.2) | 95.7 (95.7) | 96.5 (96) | 99.5 (99.5) |
| Anomalous completeness (%) | 84.2 (85) | 88 (87) | 80.3 (79.2) | ||
| Multiplicity | 3.4 (3.4) | 3.7 (3.6) | 3.5 (3.4) | 5.6 (2.3) | 6.7 (6.3) |
| Resolution for the refinement (Å) | 15.0–2.8 | 15.0–2.3 | 15.0–2.5 | ||
| Rcryst (%)/Rfree (%)b | 23/27 | 21/25 | 22/27 | ||
| R.m.s.d. (bonds) (Å)/(angles (°) | 0.0095/1.52 | 0.016/1.8 | 0.015/1.8 | ||
| No. of atoms | |||||
| protein/water | 2308/43 | 2393/130 | 2308/127 | ||
| cofactorsc | 20/1 | 36/1/1/11 | |||
| Average B-factor (Å2) | |||||
| protein/water | 53.5/60 | 50/50 | 66/68 | ||
| cofactorsc | 41/44 | 59/78/77/60 | |||
| No. of φ/ψ angles (%) | |||||
| most favoured/allowed | 80/16 | 86/12.8 | 87.1/12.5 |
The values in parentheses refer to data in the high resolution shell.
aRsym = Σhkl Σi|Ii – (I)|/Σ(I)
bRcryst = Σ(||Fp(obs)| – |Fp(calc)||/Σ|Fp(obs)| and Rfree = R-factor for a randomly selected subset (9.5%) of data that were not used to minimize the crystallographic residual.
cCofactors: UMP/Mn2+ in the case of α3GalT and UDP-Gal/-Hg/Mn2+/galactose bound to E317 in the case of α3GalT + UDPG.