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. Author manuscript; available in PMC: 2011 Oct 1.
Published in final edited form as: Nat Struct Mol Biol. 2011 Mar 6;18(4):432–436. doi: 10.1038/nsmb.2003

Table 1.

Summary of crystallographic data and refinement

Data collection 70S-EF-Tu
trp-tRNATrp
(merged from
5 crystals)
70S-EF-Tu
G24A trp-
tRNATrpUGG
(from 2 crystals)
70S-EF-Tu
G24A trp-
tRNATrpUGA
(from 2 crystals)
70S-EF-Tu
A9C trp-
tRNATrpUGA
(from 2 crystals)
Space Group P21 P21 P21 P21
Cell dimensions
a, b, c (Å) a=290.2 b=269.2
c=404.0
a=289.8 b=269.1
c=404.0
a=289.9 b=269.4
c=404.5
a=289.9 b=268.5
c=403.6
 α, β, γ (°) α=90.0 β=91.5
γ=90.0
α=90.0 β=91.2
γ=90.0
α=90.0 β=91.5
γ=90.0
α=90.0 β=91.6
γ=90.0
Resolution (Å) 50-3.1 (3.2-3.1) * 50-3.1 (3.2-3.1) 50-3.1 (3.2-3.1) § 50-3.1 (3.2-3.1)
Rsym 19.9 (115.2) 20.4 (100.9) 26.8 (130.1) 21.5 (103.3)
I/σI 7.12 (1.24) * 7.27 (1.35) 6.19 (1.23) § 10.48 (1.69)
Completeness
(%)
99.8 (99.9) 97.4 (92.7) 98.7 (98.5) 97.9 (93.2)
Redundancy 6.3 (5.2) 4.6 (4.1) 6.4 (6.5) 5.0 (4.4)
Refinement
Resolution (Å) 50.0-3.1 50.0-3.1 50.0-3.1 50.0-3.1
No. unique
reflections
1,116,606 1,087,126 1,105,502 1,090,696
Rwork/Rfree 23.7/26.4 24.7/28.5 23.8/27.5 24.3/26.7
No. atoms
 RNA 205,448 205,202 205,200 205,442
 Protein 100,888 100,888 100,888 100,888
B-factors
 RNA 99 82 90 76
 Protein 103 86 92 81
R.m.s
deviations
Bond lengths
(Å)
0.008 0.008 0.008 0.007
Bond angles (°) 1.2 1.3 1.3 1.2
*

I/σI =1.97 at 3.2 Å resolution

I/σI =2.08 at 3.2 Å resolution

§

I/σI =1.92 at 3.2 Å resolution

I/σI =2.58 at 3.2 Å resolution