Table 1.

X-ray diffraction data collection and refinement statistics for the TAZ1:fusion peptide complex

Data collection a
Beamline	ALS 5.0.3
Wavelength (Å)	0.97648
Resolution range (Å)	40.7–2.0
Space Group	P21
Unit cell dimensions (Å, °)	32.06,50.11,41.26; β=99.19
Total reflections	60265(3547)
Unique reflections	8465(562)
Rmerge (%)b	11.1(145.5)
Rmeas (%)c	12.0(158.6)
Rpim (%)d	4.5(62.4)
CC1/2 (%)e	87.8(91.0)
Completeness (%)	100.0(99.8)
Redundancy	7.1(6.4)
<I>/<σ(I)>	17.9(1.2)
Refinement
Reflections used for Rwork(Rfree)	7543(882)
Number of non-H protein atoms	1214
Number of water molecules	36
Number of Zn atoms	3
Rwork	0.2107
Rfree	0.2406
RMS (bond length)	0.003
RMS (bond angle)	0.645
Ramachandran: favored, outliers (%)	95.36,0.66
Clashscore	5.78
Wilson B-factor (Å2)	38.4
Average B-factor (Å2)	65

^aValues in parentheses are for highest resolution shell

^bR_merge = Σ_hklΣ_i=1,n|I_i(hkl)-<I(hkl)>|/Σ_hklΣ_i=1,nI_i(hkl)

^cR_mease = Σ_hkl√(n/(n-1))Σ_i=1,n|I_i(hkl)-<(I(hkl)>|/Σ_hkl|Σ_i=1,nI_i(hkl)

^dR_pim = Σ_hkl√(1/(n-1))Σ_i=1,n|I_i(hkl)-<I(hkl)->|/Σ_(hkl)Σ_i=1,nI_i=(hkl)

^eCC_1/2 = Pearson Correlation Coefficient between two random half datasets

^fNumber of unfavorable all-atom steric overlaps ≥ 0.4 Å per 1000 atoms