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

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

	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
R_work/R_free (%)	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

^aData within parentheses are for the outermost resolution shell
^bR_merge = \(\sum_{h} \sum_{\text{i}} {{\left| {I\left( h \right)_{i} - \left\langle {I\left( h \right)} \right\rangle } \right|} \mathord{\left/ {\vphantom {{\left| {I\left( h \right)_{i} - \left\langle {I\left( h \right)} \right\rangle } \right|} {\sum_{h} \sum_{i} I\left( h \right)_{i} }}} \right. \kern-0pt} {\sum_{h} \sum_{i} I\left( h \right)_{i} }}\) 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

ISSN: 2731-3654