Table 1.

Data collection and refinement statistics

	Glycosylated	endoH treated/conA purified
Crystal PDB ID	EQKM/Man-6-P 3K41	EQKM/sulfatepH7.0 3K42	EQKM/sulfatepH6.5 3K43
pH	6.5	7.0	6.5
Ligand/Mna	M6P	-	-
Data Collection
Space Group	P212121	I4	b I4
Cell Dimensions: a, b, c (Å)	53.2, 77.1, 79.9	102.6, 102.6, 100.1	103.0, 103.0, 99.8
Wavelength (Å)	1.54	1.54	1.54
Resolution (Å)	50.0–1.90(1.97–1.90)	50–2.3 (2.38–2.3)	50–2.0 (2.07–2.0)
Data collection temp (°C)	−175	−175	−175
Rsym	0.13 (0.53)	0.093 (0.481)	0.068 (0.41)
I/σI	26.7 (3.6)	20.4 (3.7)	24.7 (4.6)
Completeness (%)	99.8	99.9 (100.0)	99.7 (100.0)
Redundancy	4.2	5.2	5.7
Refinement
Resolution (Å)	50–1.90	50–2.3	50–2.0
No. of Reflections	25567	22239	344841
Rwork/Rfree	21.6/25.5	22.8/24.8	16.5/19.7
monomers/a.u.	2	2	2
Residues present in each monomer	A4-9, 16-154 B4-154	A3-10, 15-133, 141-154 B5-10, 15-154	A3-10, 15-133, 141-154 B5-10, 16-154
Total No. residues/B-average (Å2)
Protein	304/26.2	287/30.3	286/29.8
M6P	2/22.5	-	-
c NAG(Man)	4(2)/49.6	2/47.9	2/35.0
water	161/33.9	187/36.1	199/35.6
sulfate	-	8/59.2	3/54.1
imidazole	0	0	1/39.4
acetate	0	0	1/39.6
Glycerol 1-phosphate	0	2/47.2	0
RMS deviations
Bond lengths (Å)	1.29	1.2	1.2
Bond angles (°)	0.006	0.006	0.006
Ramachandran plot (No. residues/%)
Most Favorable	221/85	200/80.0	213/85.5
Additionally Allowed	39/15	48/19.2	36/14.5
Generously Allowed	0/0	1/0.4	0/0
Disallowed	0/0	1/0.4	0/0

^aAlthough Mn²⁺ was present in the crystallization media for 120805 and 041509 crystals, no appreciable Mn²⁺ peak was found in either structure.

^bTwinned with <I²>/<I>² = 1.645, twinning fraction of 0.284, and twinning operator (h, −k, −l)

^cOligosaccharide attached to Asn81; NAG, N-acetylglucosamine