Table 1

Data collection, phasing, and refinement

Data Collection Summary

Form 1 Native Apo

ATPγS soaked form

Derivative Ta₆Br₁₄

SeMet

K₂PtCl₄

Form 2 Apo

AMPPCP soaked form

Wavelength (Å)

1.0000

1.0000

1.2553

0.9792

1.0000

1.0000

1.0000

Resolution (Å)

50.0-2.40

50.0-2.40

50.0-3.00

50.0-2.50

50.0-2.60

50.0-2.00

50.0-2.7

(Highest shell)

(2.49-2.40)

(2.49-2.40)

(3.11-3.00)

(2.59-2.50)

(2.69-2.60)

(2.07-2.00)

(2.80-2.70)

Measured reflections

123829

67944

58990

101649

65378

195368

84923 (8506)

Unique reflections

31237 (3096)

29610 (3006)

16100 (1600)

27042 (2770)

24345 (2421)

51591 (4787)

22378 (2240)

Completeness

99.8 (99.7)

96.2 (98.3)

99.9 (99.9)

97.1 (100.0)

97.9 (98.2)

97.6 (91.1)

98.8 (100.0)

I/σ(I)

15.1 (7.7)

14.9 (5.3)

21.9 (6.4)

12.8 (5.8)

14.1 (5.3)

9.4 (1.8)

16.5 (6.9)

Redundancy

3.9 (3.9)

2.3 (2.2)

3.7 (3.7)

3.8 (3.8)

2.7 (2.6)

3.8 (3.2)

3.8 (3.8)

R_merge

7.1 (39.1)

7.0 (44.5)

5.3 (14.1)

7.8 (43.6)

7.4 (45.4)

7.0 (45.0)

12.0 (40.2)

MIRAS Phasing Statistics

R_iso(F) (%)

11.1

18.6

20.6

Number of Sites

8

1

5

Resolution (Å)

50.0-3.9

50.0-3.9

50.0-3.9

Phasing Power (Centric/Acentric)

0.814/0.723

1.799/1.894

1.036/0.859

Figure of merit (Centric/Acen.)

0.74/0.64

Refinement

Resolution (Å)

50.0-2.40

5.0-2.40

50.0-2.00

50.0-2.70

R_work/R_free ^a (%)

22.8/29.9

21.6/29.0

22.3/25.8

23.1/29.4

Number of atoms

Protein

5202

5374

5603

5599

Water

90

113

300

65

Ligand

25

47

-

31

Average B-factor (Ų)

Protein

41.3

38.9

27.8

37.5

Water

42.2

40.2

32.1

32.1

Ligand

60.9

58

-

71.2

r.m.s.d.

Bond Lengths(Å)

0.008

0.009

0.007

0.008

Angles(°)

1.3

1.3

1.3

1.3

PDB code

2ZJ2

2ZJ5

2ZJ8

2ZJA

^aR_free was calculated using 5% of the total reflections, which were chosen randomly and omitted from the refinement.

Oyama et al. BMC Structural Biology 2009 9:2   doi:10.1186/1472-6807-9-2