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. 2010 Jul 23;400(4):828–837. doi: 10.1016/j.jmb.2010.05.053

Table 1.

Data collection and refinement statistics for X-ray crystallography

Data collection statisticsa
Resolution (Å) 30–2.0 (2.05–2.00)
Completeness (%) 91.7 (63.9)
Multiplicity 2.7 (1.9)
II 20.2 (3.0)
Number of observations/unique reflections 690,731/74,855
Rsymb 5.1 (25.9)



Refinement statistics
Wilson B/average B 29.5/36.0
Number of non-H atoms/waters 6958/802
Number of reflections 70,789 (3611)
RMSDc bonds/angles 0.014/1.5
Ramachandrand 89.2 9.6 0.5 0.7
Rcryst/Rfreee (%) 20.0/24.3



B-factor (Å2) B-factor of equivalent domain in JM22 (Å2) RMSD with JM22 (% α-carbon residues used)
1F1E8hu 35.8 34.4 2.1 (90)
1F1E8hu Vα 35.5 28.0 1.5 (96)
1F1E8hu Vβ 36.2 27.3 1.1 (98)
1F1E8hu Cα 36.4 52.5 2.3 (78)
1F1E8hu Cβ 35.4 37.0 0.6 (99)

RMSDs were calculated using the program SHP (D. I. Stuart, unpublished).

a

Data in parenthesis are for the highest-resolution shell.

b

Rsym = σj|〈I〉 − Ij|/σ〈I〉 where Ij is the intensity of the jth reflection, and 〈I〉 is the average intensity.

c

Root-mean-square deviation from ideal values.

d

Values are expressed as the percentage of amino acids in the “core,” “allowed,” “generously allowed,” and “disallowed” regions, respectively.

e

Five percent of data have been set aside for cross-validation calculations.