IntroductionPatient progress, the movement of patients through a hospital system from admission to discharge, is a foundational component of operational effectiveness in healthcare institutions. Optimal patient progress is a key to delivering safe, high-quality and high-value clinical care. The Baystate Patient Progress Initiative (BPPI), a cross-disciplinary, multifaceted quality and process improvement project, was launched on March 1, 2014, with the primary goal of optimizing patient progress for adult patients.MethodsThe BPPI was implemented at our system’s tertiary care, academic medical center, a high-volume, high-acuity hospital that serves as a regional referral center for western Massachusetts. The BPPI was structured as a 24-month initiative with an oversight group that ensured collaborative goal alignment and communication of operational teams. It was organized to address critical aspects of a patient’s progress through his hospital stay and to create additional inpatient capacity. The specific goal of the BPPI was to decrease length of stay (LOS) on the inpatient adult Hospital Medicine service by optimizing an interdisciplinary plan of care and promoting earlier departure of discharged patients. Concurrently, we measured the effects on emergency department (ED) boarding hours per patient and walkout rates.ResultsThe BPPI engaged over 300 employed clinicians and non-clinicians in the work. We created increased inpatient capacity by implementing daily interdisciplinary bedside rounds to proactively address patient progress; during the 24 months, this resulted in a sustained rate of discharge orders written before noon of more than 50% and a decrease in inpatient LOS of 0.30 days (coefficient: −0.014, 95% CI [−0.023, −0.005] P< 0.005). Despite the increase in ED patient volumes and severity of illness over the same time period, ED boarding hours per patient decreased by approximately 2.1 hours (coefficient: −0.09; 95% CI [−0.15, −0.02] P = 0.007). Concurrently, ED walkout rates decreased by nearly 32% to a monthly mean of 0.4 patients (coefficient: 0.4; 95% CI [−0.7, −0.1] P= 0.01).ConclusionThe BPPI realized significant gains in patient progress for adult patients by promoting earlier discharges before noon and decreasing overall inpatient LOS. Concurrently, ED boarding hours per patient and walkout rates decreased.

Parallel biochemical and crystallographic studies have been carried out on the protein concanavalin B from Jack Bean (Canavalisensiformis). The studies show the protein to be a monomer of 33,000 daltons with unexceptional amino acid composition and no covalently bound carbohydrate. The molecule contains a single, firmly bound zinc ion and we present evidence that the protein specifically binds nucleotide coenzymes including at least NADPH and flavin mononucleotide. An electron density map of the concanavalin B crystals (space group P61, a = b = 80.9 A, c = 102.2 A) has been calculated from phases based on six isomorphous heavy atom derivatives. A description of the structure of the protein based on the 5.0 A resolution x-ray diffraction study is provided. The structure appears to contain a substantial amount of a-helix as well as an extensive,a-sheet and these are organized into two domains of unequal size. The position of the bound zinc is indicated by anomalous difference Fouriers and the nucleotide binding site by conventional difference Fourier maps.Concanavalin B is a protein present at substantial levels in aqueous extracts of the seeds of Canavalis ensiformis. It is one of four proteins from the Jack Bean crystallized by J. B. Summer early in this century, the others being concanavalin A (17), urease (18), and canavalin (19). The only distinctive property of concanavalin B that brought it to the attention of biochemists was its propensity to crystallize from crude solutions as long, hexagonal needles like those shown in Figure 1. Thus, it represented one of the few 'proven pure' proteins available for study. Its function in neither the seed nor the plant is known. It is not a lectin like its companion concanavalin A nor does it share other of its characteristics. Its physical and chemical properties do not place it in either the classical vicillin or legumin classes of storage proteins (2). Virtually no biochemical characterization has been attempted on concanavalin B so that its precise properties were, until this study, obscure. This is not to say that they are clear even now.Encouraged by its ease of crystallization, we initiated preliminary experiments and single crystal analyses ( 12) with the objective of elucidating its three dimensional structure. An example of its x-ray diffraction pattern is seen in Figure 2. It was determined that the space group ofthe hexagonal prisms was P61 with a = b = 80.9 A and c = 102.2 A. Electron micrographs indicated the crystals to be relatively well hydrated implying that the unit cell contained asymmetric units composed of single molecules. The mol wt of these molecules was estimated, using the ultracentrifuge, by Sumner et al. (20) Amino Acid Analysis. Three mg of protein was hydrolyzed under vacuum at 11 5C for 24 h with 6 N HCI. At the end of hydrolysis, 1.0 ml of 3.5 N NaOH was added to the hydrolysate and this was then diluted to 5.0 ml with water. One-ml aliquots containing 0.1 mg protein were applied to a Beckman 121 automated amino acid analyzer. ...

Morphological and anatomical studies have long utilized qualitative means to reconstruct 3‐dimensional transparent images from serial sections. With the advent of computer graphics systems, more accurate images can be constructed to visualize growing plant parts in transparent 3‐D. We have developed a computer program which allows such reconstruction from stained serial sections. Advantages include 3‐dimensional imaging without the use of stereo pairs and the ability to rotate an image to see all angles.

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