Table 3 PcVps75ΔC data collection and refinement statistics

From: Structural basis for the acetylation of histone H3K9 and H3K27 mediated by the histone chaperone Vps75 in Pneumocystis carinii

 

PcVps75ΔC

Data collection

Wavelength (Å)

1.000

Space group

P41

Unit-cell parameters (Å, °)

a = b = 66.4, c = 99.4;

α = β = γ = 90.0

Resolution (Å)

50.00–2.30 (2.35–2.30)

Rmergea (%)

5.0 (37.2)

Average I/σ(I)

37.1 (4.5)

No. of observed reflections

1,47,431 (8932)

No. of unique reflections

19,234 (1276)

Completeness (%)

99.8 (100)

Redundancy

7.7 (7.6)

Matthews coefficient (Å3 Da−1)

1.88

Solvent content (%)

34.49

Molecules per asymmetric unit

2

Refinement

Resolution (Å)

46.96–2.30

Rwork/Rfree

0.18/0.24

Ramachandran favored (%)

96.24

Ramachandran allowed (%)

3.49

Ramachandran outliers (%)

0.27

No. of atoms

Protein

3173

Ligand/ion

3/0

Water

94

Wilson B value

36.09

R.m.s. deviations

Bond lengths (Å)

0.009

Bond angles (°)

1.201

  1. aRmerge =\(\mathop {\sum}\nolimits_{hkl} {\mathop {\sum}\nolimits_i {\left| {I_i\left( {hkl} \right) - \left\langle {I\left( {hkl} \right)} \right\rangle } \right|/\mathop {\sum}\nolimits_{hkl} {\mathop {\sum}\nolimits_i {I_i(hkl)} } } }\), where Ii (hkl) is an individual intensity measurement, and \(\left\langle {I\left( {hkl} \right)} \right\rangle\) is the average intensity for all i reflections
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