Table 1 Cryo-EM data collection, refinement, and validation statistics

From: Structures of channelrhodopsin paralogs in peptidiscs explain their contrasting K+ and Na+ selectivities

 

HcKCR1

HcCCR

Data collection and processing

  Microscope

FEI Titan Krios

FEI Titan Krios

  Detector

Falcon 4i

Falcon 4i

  Magnification (Å)

75,000

75,000

  Voltage (kV)

300

300

  Electron exposure (e2)

40

40

  Defocus range (μm)

0.8–2.4

0.8–2.4

  Pixel size (Å)

1.03

1.03

  Symmetry imposed

C3

C3

  Initial particle images (no.)

2,685,194

2,674,318

  Final particle images (no.)

297,015

296,840

  Map resolution (Å)

2.88

2.84

  FSC threshold

0.143

0.143

  Map resolution range (Å)

2.4–3.3

2.4–3.2

Refinement

Initial model used

ab initio

ab initio

Map sharpening B factor (Å2)

−158.5

−153.1

Model composition (monomer)

  

 Nonhydrogen atoms

2330

2284

 Protein residues

240

240

 Lipids

8

9

 Water

15

15

B factors (Å2)

  

 Protein

65.80

58.81

 Lipids

71.57

62.23

 Water

68.73

54.52

R.m.s. deviations

  

 Bond lengths (Å)

0.003

0.003

 Bond angles (°)

0.449

0.447

Validation

  

 MolProbity score

1.06

1.20

 Clashscore

2.50

1.73

 Poor rotamers (%)

0

0

Ramachandran plot

  

 Favored (%)

97.90

95.38

 Allowed (%)

2.10

4.62

 Disallowed (%)

0

0