Table 1 Data collection and refinement statistics
From: Megahertz data collection from protein microcrystals at an X-ray free-electron laser
Lysozyme, 7.47 keV | Lysozyme, 9.22 keV | Concanavalin A | Concanavalin B | |
|---|---|---|---|---|
(6H0K) | (6H0L) | (6GW9) | (6GWA) | |
Data collection | ||||
Space group | P43212 | P43212 | I222 | P61 |
Cell dimensions | ||||
a, b, c (Å) | 79.9, 79.9, 38.5 | 80.1, 80.1, 38.6 | 63.9, 88.1, 90.2 | 82.3, 82.3, 103.4 |
α, β, γ (°) | 90.0, 90.0, 90.0 | 90.0, 90.0, 90.0 | 90.0, 90.0, 90.0 | 90.0, 90.0, 120.0 |
Resolution (Å) | 35–2.2 (2.3–2.2)a | 35–1.9 (2.0–1.9) | 45–2.1 (2.2–2.1) | 42–2.2 (2.3–2.2) |
R split | 0.077 (0.374) | 0.154 (0.591) | 0.128 (0.694) | 0.146 (0.560) |
CC1/2 | 0.994 (0.249) | 0.973 (0.387) | 0.984 (0.333) | 0.967 (0.232) |
CC* | 0.999 (0.631) | 0.993 (0.747) | 0.996 (0.706) | 0.992 (0.614) |
I /σ(I) | 12.0 (4.1) | 6.3 (2.9) | 7.2 (2.0) | 7.6 (3.2) |
Completeness (%) | 100.0 (100.0) | 100.0 (100.0) | 100.0 (100.0) | 100.0 (100.0) |
Multiplicity | 1160 (690) | 278 (186) | 715 (146) | 723 (241) |
Refinement | ||||
Resolution (Å) | 35.0–2.2 | 35.0–1.9 | 45.0–2.1 | 42.0–2.2 |
No. of reflections | 6717 | 10,346 | 15,227 | 20,161 |
Rwork/Rfree | 0.196/0.240 | 0.188/0.237 | 0.186 / 0.238 | 0.161 / 0.213 |
No. of atoms | ||||
Protein | 992 | 992 | 1778 | 2274 |
Ligand/ion | — | — | 2 (Ca2+, Mg2+) | — |
Water | 73 | 80 | 72 | 159 |
B-factors | ||||
Protein | 36.2 | 19.2 | 29.4 | 26.5 |
Ligand/ion | — | — | 20.9 (Ca2+), 21.8 (Mg2+) | — |
Water | 45.0 | 26.7 | 35.8 | 35.2 |
R.m.s. deviations | ||||
Bond lengths (Å) | 0.002 | 0.008 | 0.002 | 0.009 |
Bond angles (°) | 0.619 | 1.054 | 0.577 | 1.210 |
