Table 1.

Crystallographic structure determination

Crystal	Zn2+-NNQQNY	Cd2+-NNQQNY	GNNQQNY-P21	GNNQQNY-P212121
Data collection
Radiation source	Electron FEG	Electron FEG	Electron FEG	Electron FEG
Dose upper limit, e−/ Å2	5	5	5	5
Space group	P21	P21	P21	P212121
Cell dimensions
a,b,c, Å	21.5, 4.9, 23.9	22.1, 4.9, 23.5	22.9, 4.9, 24.2	23.2, 4.9, 40.5
α,β,γ, °	90, 104.0, 90	90, 104.3, 90	90, 107.8, 90	90, 90, 90
Resolution limit, Å	1.00 (1.06–1.00)	1.00 (1.05–1.00)	1.10 (1.16–1.10)	1.05 (1.11–1.05)
Wavelength, Å	0.0251	0.0251	0.0251	0.0251
No. of crystals merged	6	4	4	1
Rmerge	0.151 (0.245)	0.180 (0.282)	0.265 (0.450)	0.199 (0.586)
Rr.i.m.	0.163 (0.280)	0.203 (0.363)	0.286 (0.482)	0.230 (0.669)
Rp.i.m.	0.057 (0.111)	0.087 (0.181)	0.139 (0.223)	0.109 (0.305)
I/σI	10.2 (6.6)	7.3 (3.7)	4.6 (3.0)	4.2 (1.8)
CC1/2, %	98.5 (90.6)	96.6 (53.9)	98.4 (88.4)	98.5 (69.3)
Completeness, %	82.6 (55.3)	84.5 (66.0)	94.8 (96.0)	78.6 (79.3)
Multiplicity	7.1 (5.1)	4.6 (3.3)	6.6 (7.2)	3.7 (3.7)
Unique reflections	2,360 (202)	2,542 (257)	2,219 (326)	1,837 (257)
Refinement
Resolution range, Å	22–1.0	22–1.0	23–1.1	20–1.05
No. of reflections (work)	2,124	2,308	1,997	1,653
Rwork	0.156	0.220	0.187	0.177
Rfree	0.194	0.242	0.224	0.186
CCwork	0.955	0.922	0.954	0.966
CCfree	0.912	0.934	0.947	0.979
No. of atoms (incl. hydrogen)	111	113	114	113
Protein	97	98	107	107
Water	6	7	7	6
Cation	1	1	0	0
Acetate	7	7	0	0
B factors, Å2
Protein	4.0	4.9	4.5	4.2
Water	12.9	16.0	14.5	14.7
Cation	3.7	11.3	n/a	n/a
Acetate	4.1	17.2	n/a	n/a
Wilson B, Å2	3.2	3.4	6.1	5.7
Rms deviations
Bond lengths, Å	0.020	0.021	0.019	0.017
Bond angles, °	1.5	1.7	1.3	1.6

Numbers reported in parentheses correspond to values in the highest-resolution shell. incl., including; n/a, not applicable.