Table 1 |
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|
X-ray diffraction data collection and refinement |
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|
Data Collection Summary |
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|
|
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|
Derivative |
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|
Native |
Ta6Br14 |
SeMet |
K2PtCl4 |
||
|
Wavelength |
(Å) |
1.0000 |
1.2544 |
0.9795 |
1.0717 |
|
Resolution |
(Å) |
50.0-2.65 |
50.0-3.16 |
50.0-2.80 |
50.0-3.19 |
|
(Highest shell) |
(2.74-2.65) |
(3.27-3.16) |
(2.90-2.80) |
(3.30-3.19) |
|
|
Measured reflections |
227882 |
127012 |
181671 |
112023 |
|
|
Unique reflections |
16278 (1598) |
9676 (901) |
13780(1256) |
9034 (921) |
|
|
Completeness |
(%) |
99.4 (100.0) |
97.6 (95.1) |
99.1 (92.8) |
94.5 (99.9) |
|
I/σ(I) |
17.6 (9.9) |
23.8 (11.4) |
14.5 (7.1) |
14.2 (7.4) |
|
|
Redundancy |
14.0 (14.0) |
13.1 (13.5) |
13.2 (9.7) |
12.4 (9.3) |
|
|
Rmerge |
(%) |
4.3 (38.8) |
5.6 (23.0) |
7.5 (33.9) |
6.7 (38.6) |
|
|
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|
MIRAS Phasing Statistics |
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|
|
|||||
|
Riso(F) (%) |
12.4 |
21.1 |
17.1 |
||
|
Number of Sites |
2 |
6 |
1 |
||
|
Resolution |
(Å) |
50.0-4.0 |
50.0-4.0 |
50.0-4.0 |
|
|
Phasing Power (Centric/Acentric) |
0.56/0.57 |
0.64/0.54 |
0.63/0.62 |
||
|
Figure of merit (Centric/Acen.) |
0.32/0.36 |
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|
|
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|
Refinement |
|||||
|
Resolution |
(Å) |
50.0-2.65 |
|||
|
Rwork/Rfreea |
(%) |
25.7/29.7 |
|||
|
Number of atoms |
|||||
|
Protein |
2623 |
||||
|
Water |
33 |
||||
|
Average B-factor |
(Å2) |
||||
|
Protein |
65.7 |
||||
|
Water |
56.9 |
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|
r.m.s.d. |
|||||
|
Bond Lengths |
(Å) |
0.01 |
|||
|
Angles |
(°) |
1.364 |
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|
PDB code |
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|
|
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|
aRmerge = (Σ|II < II > |)/ΣI |II|, where < II > is the mean II over symmetry-equivalent reflections. bRwork =Σ|FO - FC |/Σ|FO| for all data excluding data used to calculate Rfree. cRfree was calculated using 5% of the total reflections, which were chosen randomly and omitted from the refinement. |
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|
Oyama et al. BMC Biology 2011 9:28 doi:10.1186/1741-7007-9-28 |
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