Table 1.

Data collection and refinement statistics (molecular replacement)

	a	b	c	Comb (a,b,c)
Data collection
Space group	P43a	P43a	P43a	P43a
Cell dimensions
a/b, c (Å)	106.55, 122.23	106.19, 120.76	106.32, 120.74	106.59, 122.30
Resolution (Å)	30.0−2.90 (3.00−2.90)	30.0−2.90 (3.00−2.90)	30.0−2.90 (3.00−2.90)	30.0−2.90 (3.00−2.90)
Rsym or Rmerge	0.063 (0.340)	0.063 (0.423)	0.064 (0.521)	0.088 (0.501)
I/σI	9.98 (1.35)	10.0 (1.31)	11.2 (1.30)	14.1 (1.80)
Completeness (%)	58.4 (60.0)	56.9 (58.3)	46.3 (47.6)	91.3 (92.4)
Redundancy	1.2 (1.1)	1.3 (1.2)	1.2 (1.2)	2.2(2.1)
Refinement
Resolution (Å)				30.0−2.90
No. reflections				25 538
Rwork/Rfreeb				0.228/0.250
No. atoms				6 868
Protein				6 863
Ligand/ion				5(1 PO4− ion)
Water				0
B-factors
Protein				52.02
Ligand/ion				53.78
Rmsd
Bond lengths (Å)				0.008
Bond angles (°)				1.236
Ramachandran plotc
Favored (% residues)				90.7
Allowed (% residues)				9.3
Disallowed (% residues)				0

^aThe crystals are P4₃ but are hemihedrally twinned and appear to be P4₃2₁2, with twin operator −h, k, −l and twin fraction 0.478.

^bTwinned R_work/R_free from Refmac5 (22).

^cDetermined using PROCHECK (46).