The LeFort I osteotomy has become a routine procedure in elective orthognathic surgery. The authors report the occurrence of intra- or perioperative complications in a series of 1000 consecutive LeFort I osteotomies performed within a 20-year period. In total, 64 (6.4%) patients experienced complications. Anatomical complications affected 26 (2.6%), patients, including 16 (1.6%) with a deviation of the nasal septum and 10 (1.0%) with non-union of the osteotomy gap. Extensive bleeding that required blood transfusion occurred in 11 (1.1%) patients exclusively after bimaxillary corrections; in 1 patient a ligation of the external carotid artery became necessary. Significant infections such as abscesses or maxillary sinusitis occurred in 11 (1.1%) patients. No patient experienced an osteomyelitis. Ischemic complications affected 10 (1.0%) patients, including 2 (0.2%) who experienced an aseptic necrosis of the alveolar process and 8 (0.8%) who, under critical revision, were affected by retractions of the gingiva. Five (0.5%) patients experienced an insufficient fixation of the osteosynthesis material. The risk and the extent of complications was enhanced in patients with anatomical irregularities (eg, in patients with craniofacial dysplasias, orofacial clefts, or vascular anomalies). The risk of ischemic complications was enhanced in extensive dislocations or transversal segmentation of the maxilla. The authors conclude that patients with major anatomical irregularities should be informed about an enhanced risk of Le-Fort I osteotomies. Preoperative planning avoiding transversal segmentation or extensive dislocations of the maxilla should reduce the occurrence of complications. For healthy individuals, the risk of complications with the LeFort I osteotomy is considered low.

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The Hsp90 chaperone is a central node of protein homeostasis activating a large number of diverse client proteins. Hsp90 functions as a molecular clamp that closes and opens in response to the binding and hydrolysis of ATP. Crystallographic studies define distinct conformational states of the mechanistic core implying structural changes that have not yet been observed in solution. Here, we engineered one-nanometer fluorescence probes based on photo-induced electron transfer into yeast Hsp90 to observe these motions. We found that the ATPase activity of the chaperone was reflected in the kinetics of specific structural rearrangements at remote positions that acted cooperatively. Nanosecond single-molecule fluorescence fluctuation analysis uncovered that critical structural elements that undergo rearrangement are mobile on a sub-millisecond time scale. We identified a two-step mechanism for lid closure over the nucleotide-binding pocket. The activating co-chaperone Aha1 mobilizes the lid of apo Hsp90, suggesting an early role in the catalytic cycle.

The in vitro activities of 16 antimicrobial agents against 180 Acinetobacter strains isolated from blood cultures (n = 162), central venous catheters (n = 11), and cerebrospinal fluids (n = 7) were studied. MICs were determined by a microtiter broth dilution method. Considerable differences in antimicrobial drug susceptibility against strains belonging to different species could be demonstrated. Acinetobacter baumannii isolates (n = 108) were generally more resistant than isolates identified as species other than A. baumannii. Multidrug resistance was common among A. baumannii isolates. Of the antimicrobial agents tested, imipenem was highly active against all A. baumannii isolates, and the other agents tested were only moderately active or inactive. Good activity against Acinetobacter species strain 3 was demonstrated for imipenem, amikacin, and ciprofloxacin.Most of the strains belonging to other species were susceptible to imipenem, ciprofloxacin, expanded-spectrum cephalosporins, amoxicillin-clavulanate, and the aminoglycosides but were resistant to ampicillin and older cephalosporins.

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