Table 1.
(A) Presence of CCSC in cryo-EM reconstructions of HSV-1 capsids, and (B) Mass spectrometric analysis of bands from SDS-PAGE of capsids.
| A: | ||||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| Type of capsid | Resolution (Å) [1] | No. of particles | CCSC occupancy [2] | Copy number | ||||||
| C-capsids | 19.9 (0.5) 17.6 (0.3) | 643 pairs | 0.54, 0.55 (0.55) | 33 | ||||||
| C-capsids | 26.8 (0.5) 24.5 (0.3) | 538 | 0.45, 0.44 (0.45) | 27 | ||||||
| A-capsids (wildtype) [3] | 22.9 (0.5) | 2111 | 0.15, 0.07 (0.11) | 7 | ||||||
| A-capsids (wildtype) [3, 4] | 27.5 (0.5) 26.8 (0.3) | 1100 | 0.18, 0.08 (0.13) | 8 | ||||||
| A-capsids (UL25-null) | 22.7 (0.5) 21.9 (0.3) | 1088 | 0.00, 0.00 (0.00) | 0 | ||||||
| C-capsids (+ 0.5M GHCl) | 25.0 (0.5) 24.1 (0.3) | 595 | 0.00, 0.00 (0.00) | 0 | ||||||
| B : | ||||||||||
| Protein | M.W | peptides matched/submitted | coverage | AMD [5] | Score [6] | P value [7] | ||||
| UL6 | 74,046 | 10/20 | 23% | 0.009 | 127 | 1.99E-13 | ||||
| UL17 | 74,536 | 9/12 | 16% | 0.012 | 105 | 3.16E-11 | ||||
| UL25 | 62,631 | 19/28 | 45% | 0.017 | 211 | 7.93E-22 | ||||
| UL36 (VP1/3) | 335,655 | 33/59 | 15% | 0.017 | 155 | 3.16E-16 | ||||
Resolution is according to the Fourier Shell Correlation, thresholded at 0.5 or 0.3.
The two numbers correspond to measurements made in the vertex-distal and the vertex-proximal parts of the CCSC and (in bold), their mean.
reported by Cheng et al (2002)
In this reconstruction, grayscale sections show some faint density at the CCSC site, but it is at the level of background noise. If genuine, it would correspond to an occupancy of 3-fold to 4-fold lower than is observed on C-capsids.
Average mass deviation (absolute values) in Daltons for all matched peptides from theoretical peptides
Score is determined as −10*LOG10(P)
P is a probability-related measure that the identified protein is a random match