. Author manuscript; available in PMC: 2010 Apr 6.

Published in final edited form as: Nat Struct Mol Biol. 2009 Dec 20;17(1):38–43. doi: 10.1038/nsmb.1753

Table 1.

Data collection and refinement statistics (molecular replacement)

Data collection	PHF8 (residues 1–447)	KIAA1718 (residues 1–488)		KIAA1718 (residues 92–488)
Cofactors	Zn²⁺, Fe²⁺, N-oxalylglycine	Zn²⁺, Fe²⁺, N-oxalylglycine	Zn²⁺, Fe²⁺, α-ketoglutarate	Fe²⁺	Fe²⁺, α-ketoglutarate	Fe²⁺, N-oxalylglycine
Peptide	H3(1–24)K4me3-K9me2
Space group	P4₃2₁2		P2₁2₁2₁		P6₁22
Cell dimensions	(α= β= γ= 90°)		(α= β= γ= 90°)		(α= β= 90°, γ= 120°)
a, b, c (Å)	73.5, 73.5, 210.8	62.7, 125.6, 206.1	63.4, 125.2, 206.0	77.9, 77.9, 289.7	78.1, 78.1, 290.8	78.3, 78.3, 289.1
Resolution (Å)	34.72–2.19 (2.27–2.19)^a	34.82–2.39 (2.48–2.39)	34.54–2.89 (2.99–2.89)	34.32–2.29 (2.37–2.29)	34.40–2.79 (2.89–2.79)	33.67–2.69 (2.79–2.69)
R_merge	0.035 (0.647)	0.055 (0.637)	0.119 (0.557)	0.089 (0.793)	0.088 (0.381)	0.085 (0.394)
I/σI	7.2 (2.3)	9.7 (1.7)	16.5 (4.0)	21.9 (4.2)	15.5 (4.1)	13.3 (2.6)
Completeness (%)	100.0 (99.9)	94.8 (81.3)	97.6 (95.6)	99.8 (100)	99.5 (99.3)	98.3 (86.3)
Redundancy	6.2 (5.7)	8.0 (4.2)	7.8 (7.4)	11.1 (11.9)	7.0 (7.3)	14.4 (8.0)
Refinement
Resolution (Å)	2.19	2.39	2.89	2.29	2.79	2.69
No. reflections	28,629	57,397	35,289	23,158	12,680	14,477
R_work/R_free	0.217/0.255	0.216/0.245	0.215/0.253	0.222/0.258	0.203/0.269	0.216/0.267
No. atoms
Protein	3,564	7,084	7,145	2,922	2,925	2,931
Heterogen	56	17	30	4	14	14
Water	206	329	166	111	50	38
B-factors (Å²)
Protein	25.7	41.0	32.7	42.9	47.3	53.9
H3 peptide	22.1
Cofactor	32.0	75.5	82.2	57.0	69.3	92.6
Water	29.8	37.5	22.6	47.1	40.7	41.0
R.m.s. deviations
Bond lengths (Å)	0.006	0.006	0.008	0.009	0.007	0.006
Bond angles (°)	1.2	1.3	1.3	1.4	1.3	1.3

Values in parentheses are for highest-resolution shell.