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Table 3 X-ray diffraction data and refinement statistics for the TatCel7A_CD structures

From: Correlation of structure, function and protein dynamics in GH7 cellobiohydrolases from Trichoderma atroviride, T. reesei and T. harzianum

  Apo structure (APO) Thio-cellotriose complex (SG3)
Data collection
 PDB accession no. 5O5D 5O59
 Beam line I911-3, MAX-lab ID23-1, ESRF
 Space group
 Cell dimensions
P21 P21
 a, b, c (Å) 56.17, 71.67, 104.22 55.85, 71.34, 102.91
 Wavelength (Å) 1.0 1.0
 Resolution (Å)a 34.74–1.72 (1.82–1.72) 58.63–1.75 (1.85–1.75)
 Unique reflections 87,266 67,271
 Multiplicity 5.2 (4.6) 2.8 (2.9)
 Completeness (%) 99.9 (99.6) 83.5 (79.1)
 I/σI 9.2 (3.4) 8.8 (2.3)
 R merge (%)b 13.2 (44.0) 8.7 (50.4)
Refinement
 Rwork/Rfree (%) 14.8/17.3 15.6/19.0
 Protein atoms: no., average B-factor (Å2) 6571
17.9
6531
18.1
 RMSD Bond angle (°) 1.052 1.353
 RMSD Bond length (Å) 0.0051 0.008
  1. aData within parentheses are for the outermost resolution shell
  2. bRmerge = \(\sum_{h} \sum_{\text{i}} {{\left| {I\left( h \right)_{i} - \left\langle {I\left( h \right)} \right\rangle } \right|} \mathord{\left/ {\vphantom {{\left| {I\left( h \right)_{i} - \left\langle {I\left( h \right)} \right\rangle } \right|} {\sum_{h} \sum_{i} I\left( h \right)_{i} }}} \right. \kern-0pt} {\sum_{h} \sum_{i} I\left( h \right)_{i} }}\) where I(h) i is the intensity of reflection h and \(\left\langle {I\left( h \right)} \right\rangle\) is the average value over multiple measurements