Table 1

X-ray diffraction data collection and refinement

Data Collection Summary


Derivative

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)


MIRAS Phasing Statistics


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


Refinement

Resolution

(Å)

50.0-2.65

Rwork/Rfreea

(%)

25.7/29.7

Number of atoms

Protein

2623

Water

33

Average B-factor

2)

Protein

65.7

Water

56.9

r.m.s.d.

Bond Lengths

(Å)

0.01

Angles

(°)

1.364

PDB code

3ANW


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.

Oyama et al. BMC Biology 2011 9:28   doi:10.1186/1741-7007-9-28

Open Data