Effect of print orientation on the dimensional accuracy of orthodontic aligners printed 3-dimensionally.

INTRODUCTION: Fabrication of orthodontic aligners directly via 3-dimensional (3D) printing presents the potential to increase the efficiency of aligner production relative to traditional workflows; however tunable aspects of the 3D-printing process might affect the dimensional fidelity of the fabricated appliances. This study aimed to investigate the effect of print orientation on the dimensional accuracy of orthodontic aligners printed directly with a 3D printer. METHODS: A digitally designed aligner of 500 µm thickness was printed in 3D in Grey V4 (Formlabs, Somerville, Mass) resin at 8 angulations at 45° intervals (n = 10 per angulation) using a stereolithography 3D printer. Each aligner was scanned with an optical scanner, and all but the intaglio surface of each scan was digitally removed. Each resultant scan file was superimposed onto the isolated intaglio of the designed master aligner file. The dimensional deviation was quantified with Geomagic Control software (3D Systems, Rock Hill, SC), and data were analyzed using R statistical software (version 2018; R Core Team, Vienna, Austria) (P <0.05). RESULTS: Print angle showed a statistically significant effect on standard deviation, average positive deviation, absolute average negative deviation, and percentage of points out of bounds (tolerance bounds defined as ±250 µm) (P <0.05). Qualitative analysis of the 3D surface deviation maps indicated that the 0° and 90° groups showed less deviation and appeared to be the most accurate in the anterior regions. Overall, the majority of the print angle groups studied were not printed within clinically acceptable tolerance ranges, with the major exception being the 90° group, which printed nominally within clinically acceptable tolerance ranges. CONCLUSIONS: With the workflow applied, print orientation significantly affects the dimensional accuracy of directly 3D-printed orthodontic aligners. Within the limitations of this study, printing at the 90° angulation would be advised as it is the group with the most accurate prints relative to the 7 other orientations investigated, although not all differences were statistically significant.

Structural analysis of bacteriophage T4 DNA replication: a review in the Virology Journal series on bacteriophage T4 and its relatives.

The bacteriophage T4 encodes 10 proteins, known collectively as the replisome, that are responsible for the replication of the phage genome. The replisomal proteins can be subdivided into three activities; the replicase, responsible for duplicating DNA, the primosomal proteins, responsible for unwinding and Okazaki fragment initiation, and the Okazaki repair proteins. The replicase includes the gp43 DNA polymerase, the gp45 processivity clamp, the gp44/62 clamp loader complex, and the gp32 single-stranded DNA binding protein. The primosomal proteins include the gp41 hexameric helicase, the gp61 primase, and the gp59 helicase loading protein. The RNaseH, a 5' to 3' exonuclease and T4 DNA ligase comprise the activities necessary for Okazaki repair. The T4 provides a model system for DNA replication. As a consequence, significant effort has been put forth to solve the crystallographic structures of these replisomal proteins. In this review, we discuss the structures that are available and provide comparison to related proteins when the T4 structures are unavailable. Three of the ten full-length T4 replisomal proteins have been determined; the gp59 helicase loading protein, the RNase H, and the gp45 processivity clamp. The core of T4 gp32 and two proteins from the T4 related phage RB69, the gp43 polymerase and the gp45 clamp are also solved. The T4 gp44/62 clamp loader has not been crystallized but a comparison to the E. coli gamma complex is provided. The structures of T4 gp41 helicase, gp61 primase, and T4 DNA ligase are unknown, structures from bacteriophage T7 proteins are discussed instead. To better understand the functionality of T4 DNA replication, in depth structural analysis will require complexes between proteins and DNA substrates. A DNA primer template bound by gp43 polymerase, a fork DNA substrate bound by RNase H, gp43 polymerase bound to gp32 protein, and RNase H bound to gp32 have been crystallographically determined. The preparation and crystallization of complexes is a significant challenge. We discuss alternate approaches, such as small angle X-ray and neutron scattering to generate molecular envelopes for modeling macromolecular assemblies.